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Contents Page 3

Organic is Better – Wendy Leung 12D

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Influenza – The End of the World – Priscilla Lee 11F

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Human Pigmentation – The Science Behind Color – Grace Zheng 9F

Page 10 What is a Higgs Boson? – Aileen Bai Yang 9D Page 12 Antimatter: What is it? – Rohan Daswani 11F Page 14 Martians…? – Suneh Bhatia 10F Page 16 Hyperloop: The future of transport – Matthew Wright 12W Page 18 Learn to Paint like Van Gogh Overnight – Angie Wong 12F Page 20 T-Cell Therapy: A Cure for Cancer? – Mallika Laul 12F Page 23 The Beginning of Genome Editing – Megan Lee 12F Page 25 Epigenetics: Famine passed down generations – Alice Zhang 12R Page 27 Role of Bone hormone in glucose production – Miyu Terashima 12N Page 29 Bibliographies

Editors: Sotaro Ogawa 12R, Darren Mok 12F, Matthew Wright 12W Cover Art: Eytan Cohen 12N 2


Organic is Better Wendy Leung 12D

Organic. Much more nutritious, good for the environment, good for the animals, the best kind of ingredient, better than everything else on the shelves. Always the best option. Such is the conventional view on organic farming and organic products. However, is organic produce actually “better�? Organic farming is the farming of crops or livestock without synthetic inputs such as fertilizers, pesticides, herbicides, regulators and genetically modified organisms. On the other hand, industrial farming is any agricultural system which uses synthetic inputs. This results in higher quality soil and harvests. Fertilizers Synthetic fertilizers contain nutrients that plants can easily take up as they are water-soluble, thus they are fast acting and effects can be seen immediately. However, this also means it is much more susceptible to leaching away, which is the process by which the fertilizers travel away from the crop. If those synthetic fertilizers reach bodies of water, eutrophication may occur, causing massive algae growth on the surface of the water, eventually blocking sunlight and oxygen for the underwater plants and wildlife, damaging the ecosystem. They are readily available in large amounts allowing farmers to purchase them at a lower price. These fertilizers can also be customized to suit the environment and crop, making it much more effective.

Another Perspective: Conventional Farming and Genetically Modified Organisms Another alternative to organic farming is genetically modified crops, which reduces herbicide and pesticide use, and are generally hardier and less susceptible to climate change and spoilage. GMO farming has its own fair share of problems, however it produces higher yields and is more efficient than organic farming as a whole. Another benefit of GMOs is that nutritional value can be added, for example, golden rice, in which β-Carotene is produced, and is synthesized as Vitamin A in the human body, preventing Vitamin A deficiency in some countries.

Unlike their synthetic counterpart, organic fertilizers such as compost and manure releases nutrients slower than the rate at which plants use them up, thus they are less susceptible to leaching. Using organic fertilizers also improves soil fertility and texture, as it contains organic material which feeds helpful microorganisms. Although organic fertilizers improve the soil quality, untreated manure poses a health and safety issue to humans due to the possible pathogens in them. One common solution to this is to compost the manure, which takes some more processing, which releases more greenhouse gases.

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Herbicides and Pesticides It’s natural to want to avoid consuming pesticides and herbicides. Since these chemicals are used to kill, it’s also natural to assume that they pose threat to our own lives (which may or may not be true). One well known case of this is the usage of DDT as an insecticide in the 1960s, which accumulated in the food chain of the local ecosystems, resulting in the egg shells of birds to become very thin, greatly reducing the bird population and threatening ecosystem balance. However, they are also extremely useful to farmers, as they protect the crops from other competitors and dangers, increasing their yield and allowing them to have more income. Overall, the tradeoff between the health of the people and overall yield of food is debatable.

more energy, which often comes from burning fossil fuels, which releases loads of carbon dioxide into the atmosphere. Resources Organic farming uses more resources, in a world where resources are scarce. As global population increases, more food has to be produced on the same area of available land. Organic farming requires a larger area of land and requires more water to keep that land fertile. Yield produced by organic is also much lower than that of synthetic farming, as with synthetic farming every aspect of the farming process can be customized to suit the environment crop to maximize efficiency. It is also a common belief that organic crops may have higher nutritional value than their conventional counterparts, although this has not been conclusively proven.

Greenhouse Gas Release In a world where global climate change is of major concern, the need for the reduction of greenhouse gases is increasing. However practices of organic farming releases greenhouse gases into the atmosphere. To maintain the soil quality and to reduce soil erosion, the soil is tilled and overturned frequently, compared to conventional farming, which releases the methane gas produced by the decomposing organic material in the soil. Since synthetic nitrogenous fertilizers cannot be used, organic farmers opt for organic fertilizers such as manure and compost. The production of compost includes decomposition of food waste which also releases methane. Methane is 24 times more potent than carbon dioxide as a greenhouse gas. On the other hand, the production of synthetic fertilizers uses a lot

Conclusion While organic farming may indeed be better for individual consumption, it is too inefficient to be the way forward for feeding the world/solving world hunger. It most likely will remain a luxury product for those who can afford them.

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Influenza – The End of the World Priscilla Lee 11F

released, infecting other cells. Eventually, the infected reach the blood streams, spreading the virus all over the body. It is at this point that the victim starts to experience symptoms such as sneezing, coughing, fever, which is the body’s defensive response to the invading viruses. If left untreated, the virus continues to attack the body, causing gastric problems, neurological problems, pneumonia, multiorgan failure, and ultimately, death.

When people think of the end of the world, most tend to think of nuclear war, global warming, or even an AI uprising. However, many often neglect the hidden threat, one of the main killers of children and adults alike in recent history -- influenza. Surprisingly, out of the many mass murderers of the last century, the most truly terrifying one is not Hitler or Stalin, but a seemingly innocuous virus that killed 20 - 40 million people in a single year. How could a single virus cause so many deaths in such a short amount of time? What makes this virus so uniquely deadly?

What is it? The virus that caused this disaster is known specifically as Influenza A. Commonly carried by birds and pigs, the disease is occasionally transmitted to humans through direct contact with the infected. Then, the disease can be transmitted between humans through coughing and spit. How does Influenza A infect the human body? The virus is covered in spike-like protrusions, which are called keys. When it enters the lungs, they land on the host cell, which are covered in lumps called ‘locks’. If the ‘key’ fits into the ‘lock’, the virus is allowed into the cell. From then on, the virus will try to produce more copies of itself, through an enzyme called polymerase. The virus controls this enzyme to produce more copies of its genetic material within the host cell. However, to truly control the cell, the virus needs to copy its RNA (genetic material) into mRNA (messenger RNA) of the host cell, which is then turned into viral proteins. To do so, the viruses use the infected polymerase to cut off a small chain of RNA called a ‘cap’, which works like a tag. The ‘cap’ is then stuck onto the end of the mRNA strand with polymerase, which tells ribosomes of the host cell to turn the tagged mRNA into protein. This process is called ‘cap-snatching’.

What makes influenza so much more dangerous than other viruses? Firstly, influenza is dangerous because scientists still do not know much about it. Despite the advances in modern technology, there are still many unanswered questions about the influenza virus. The lack of preparation is also another problem -- many governments and citizens still do not take the necessary precautionary measures (e.g. Washing hands, installing a clean water system) to prevent outbreaks. Even during pandemics, there are still countries who refuse to kill the infected carriers (namely chicken and other poultry), fearing dissatisfaction from corporations and the general populace.

This process continues until the host cell explodes from the sheer number of viral proteins. The virus is

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Most importantly, however, the influenza virus is dangerous because it mutates -- rapidly and frequently. This means that every few years, the influenza virus will strike back in a different form that people are unprepared for. This sudden shift is called the ‘antigenic shift’, where different viruses combine to form a new subtype. Existing vaccines will be useless, as they do not target that specific type of mutation and there are often no vaccines for the new strains. Creating a vaccine will take at least 3 months, and by that time, the peak of the pandemic will already have passed. Scientists can only guess what type of mutation will emerge next, but there is no guarantee.

However, it is only a matter of time before a mutation emerges that does have the right ‘key’. When this happens, scientists estimate that up to 20% of the entire human population may be wiped out. Our hospital capacities would still be overwhelmed and despite all our medical technology, without the vaccine, the death toll would most definitely skyrocket.

Prevention? The best way to prevent influenza is to stay away from live animals such as pigs or birds, as they are often the carrier for the virus. Regular hand-washing and maintenance of hygiene is also very important to get rid of germs and viruses that may be stuck to the body. Apart from that, it is also very important to avoid close contact with sick people, especially if they are coughing or sneezing. If you are feeling unwell, do not linger around other people, as that increases the chance of others getting infected. Arrange a check up at the nearest clinic as soon as possible, and wear a mask.

Studies have also shown that there is a drastic increase in the birth of new strands of influenza. After the disastrous Spanish Flu in 1918 that killed 20 - 40 million people, it took almost 4 decades for the next subtype to emerge. However, in recent years, it took only 2. Some forms of the virus, such as H5N1, also have a high fatality rate, killing 60% of those infected.

It is also important to keep healthy -- whilst the pandemic is not here yet, having a strong body will increase your chances of survival. You may also choose to take some existing vaccines to help you build up your immunity against the older strains of influenza. Many governments are starting to stockpile different vaccines against the most dangerous strains of influenza, such as H1N1, H4N1 or H7N9, but even so, there is still no guarantee that these vaccines will provide any cure for the patient.

Right now, the only barrier preventing a global pandemic, is the fact that many influenza types do not spread easily. This is because most ‘keys’ on the virus do not fit the ‘locks’ of the human cell very well.

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Human Pigmentation – The Science Behind Color Grace Zheng 9F

IN OUR FAST-PACED MO DERN SOCIETY, SKIN CO LOR HAS ALWA YS REMAIN ED A SENSITIVE TOPIC. IN MOST CITIES NOWADAYS, YO U CAN STEP OU T ON TO THE STREETS AN D EXPECT TO SEE PEOPLE O F DIFFERENT CO LORS. FROM OUR H AIR TO OUR EYES, WHAT IS IT THA T GIVES US OUR LARG E V ARIETY O F SHADES?

Effects of Melanin The amount of melanin found in your skin often dictates your skin color; people who have no melanin can develop a condition known as albinism. This is due to the absence of the oxidase tyrosinase which is a key element of the reaction the produces melanin. Normally you would inherit several genes from your parents that would decide your skin color. However, it is much more complicated than mixing colors like how you normally would when you paint. Whether the traits are dominant or recessive can play a role too; for example, if one of your parents have brown eyes and the other has blue, you are likely to have brown eyes as that trait is more dominant. Nonetheless, your skin color can be constantly changing throughout your life. For example, when you sun-tan, the melanocytes produce more melanin because it protects your skin from burning. Your skin will then appear either redder or darker because the levels of melanin in your skin have now increased. Other causes that might lead to a change in skin color include cancer, vitiligo and at times even pregnancy. Melanin can bring a lot of benefits to the human body depending on where you live. Dark skinned people often have more eumelanin, which not only gives a better protection against ultraviolet rays but helps decrease the chance of contracting diseases like skin cancer. However, the prevention of ultraviolet rays isn’t always beneficial. A research conducted showed high levels of melanin in your body could increase your risk for vitamin D deficiency if you lived in places where there was little sunlight, such as areas

When you were young, you were probably told to put a hat on before you left the house to avoid the sun's rays – this is because in the human skin, ultraviolet rays can trigger a reaction called melanogenesis which causes the skin to darken. Our skin can be divided into three basic layers, the epidermis, the dermis and the hypodermis. The outer layer is the epidermis which acts as a layer of protection that prevents and blocks out infections. The dermis helps us feel as it contains mechanoreceptors, and the hypodermis is used to store fat in the human body. In the basal layer of the epidermis, there are cells called melanocytes which produce a pigment called melanin. Melanocytes were first discovered around the 19th century by European physicians trying to understand the science behind human pigmentation. These pigments later turned out to be derivatives of tyrosine, an amino acid. Later it was found that melanin appeared not only in our skin but in our hair, ears and even parts of our brain as well! So how do the different amounts of melanin in our body affect us?

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away from the equator. This is because vitamin D is obtained naturally through sunlight, and as melanin can absorb these rays people with darker skin are more prone to rickets (a skeletal disorder) if they do not get enough vitamin D. In the eye, melanin also plays an extremely important role. Melanin can be found in cells in the eye and they help absorb any light that may have passed the retina. This will allow better visual acuity because by absorbing the light scattered within the eyeball, it will prevent the light from being reflected back. Types of Melanin In the brain, the third type of melanin can be found; neuromelanin. Even today, a lot about neuromelanin remains unknown. Scientists know that it is produced in some areas of the brain, but other than that, not much was known about it However, recently there has been renewed interest in this pigment due to a speculation that there is a connection between neuromelanin and the death of neuron cells which, for example, occurs in people with Parkinson’s disease (a neurodegenerative disorder). Neuromelanin may also give particular brain sections its color, and interestingly, the pigment can be found in some primates as well, even though more neuromelanin is present in the human brain than any other primate. Further studies hope to establish more information on the connection this specific type of melanin has to Parkinson’s disease.

There are mainly two types of melanin; the first one being eumelanin which displays a range of brown skin tones including brown, blonde and black hair. The second is pheomelanin and it gives an orange-red color which can be seen in freckles as well. Depending on how many granules of each pigment you have, your hair color can either be jet black or white-blonde. The amount of melanin you have may be dependent on your ethnicity. A study showed that Chinese and Europeans skin types had approximately half of the amount of the epidermal melanin that was found in the African and Indian skin types (which were darkly pigmented). A mix of melanin can also be found in hair, giving us the diverse range of colors, we see today.

Conclusion Through years and years of evolution, humans have taken on a large number of hues. Depending on where you live and your biological origins, everyone is unique. Sometimes, it even acts as a clue to someone’s ancestry. However, it is important to keep in mind that a person’s race does not define their character, and the next time a question about skin color is raised, you will know the science behind it.

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What is a Higgs Boson? Aileen Bai Yang 9D

of 4 forces: Strong, weak, electromagnetic and gravity. The Standard Model has helped us a lot by giving us a better insight on what was going on and what had happened in our universe. However, the standard form fails to explain how particles get their mass and why same sized particles could have different masses. This is where Peter Higgs’ theory comes in. The Higgs Boson and the Higgs Field is the missing piece to the standard model.

It has always been a wonder to many scientists how different particles obtained their different masses. In 1964, Peter Higgs suggested a theory that there is an energy field that gives each particle its mass.

The theory suggested by Peter Higgs was that particles that interacted a lot with this energy field would have a bigger mass than particles that don’t interact with the energy field as much. This meant that particles actually gain mass by passing through an energy field and the more it interacts with this field the more mass is gained. This energy field was named the Higgs Field after the physicist who suggested the theory. It is believed that the Higgs Field exists everywhere in our universe.

There is something called a standard model, where physicists are trying to break down the complications of our universe into something much more basic and simple. They are trying to find out what the universe is made of, how it was made and much more. The standard model talks about the forces that make up our universe and the particles as well. We have obtained so much information from this already by finding out about atoms, protons, electrons, neutrons, quarks (makes up protons and neutrons) and leptons (negatively charged particles).

So how is the Higgs Boson related to the Higgs field? Well the Higgs field is made up of countless Higgs Bosons. A Higgs Boson consists of subatomic particles that when joined together creates a Higgs Field. Scientists believe that the Higgs field is what gives matter its mass.

According to the standard model our universe is made of 12 different particles, where 6 are quarks and 6 are leptons. Along with that our universe it also made up

The way the Higgs Bosons work is that as particles float around this energy field they will interact with the Higgs Bosons as well as attract them. Some particles

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may attract and interact with a large bunch of Higgs Bosons while other particles might attract few to none! And what scientists have concluded is that the more Higgs Bosons the particles interact with and attract, the more mass is gained on the particle. This explains how 2 particles with the same size can have different masses.

The Higgs Boson is an important part of the universe; it is something we can’t do without. We have gone a long way from knowing absolutely nothing to now, but there is still so much more out there scientists have not yet discovered. Luckily, with our technology getting more and more advanced, scientists will most likely find out more in the near future.

If we didn’t have the Higgs field there would be no atoms, and single particles would just fly around at the speed of light. Our universe would not be the way it is right now without the Higgs field and the Higgs Boson. Without the Higgs field we would all disintegrate, not to mention that we would break apart at the speed of light. The Higgs field acts like glue, it holds us together. In short without the Higgs field our universe would be a chaotic mess – a disaster. This just shows us how important and powerful the Higgs Boson is and how much it can benefit and support all living things (and non-living things) in the universe.

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Antimatter: What is it? Rohan Daswani 11F

If our universe had equal amounts of matter and antimatter, the universe as we know it would cease to exist as soon as matter met its antimatter component. In our universe, matter is the norm, but some may speculate that if there’s no antimatter here it must be somewhere else. So far, there is no scientific evidence to support parallel anti-universes. However if there are anti-universes, it is best that we stay far, far away from them.

Matter merely is everything around you. If something has a mass and takes up space, it is defined as matter. However recent discoveries have found a new substance; it goes by the name of antimatter. In laymen’s terms, antimatter is just the opposite of any matter. Antimatter matches the average particle almost precisely except for its opposite charge. It is believed that during the Big Bang, equal amounts of matter and antimatter were created. However, merely looking around raises a question: “Where did all the antimatter go?” In 1928, Dirac spent his time working on an equation combing both special relativity and quantum theory as he tried to interpret the “behavior of an electron moving at relativistic speed” (an electron moving at a velocity comparable to the speed of light). However, his equation posed one problem: there were two solutions to Dirac’s equation, one for electrons with positive energies, and one for electrons with negative energies. Similar to how the equation x2 = 4 has two possible solutions, x = 2, and x = -2. Dirac then made a surprising prediction—for every particle in the universe there would have to exist an antiparticle—a notion unheard of in the science community. Four years later, Carl Anderson, a physicist from Caltech discovered the first ever antiparticle while studying the effect that cosmic rays have when they collide with the nucleus of an atom. During his research, Anderson noticed particles he had never seen. These particles were almost identical in all aspects to an ordinary particle, except for an opposite charge. He first identified them as “antielectrons”; hence, the infamous name, positrons. Fast-forward to 1995, the European Centre for Nuclear Research (CERN) formed the first ever antiatoms, antihydrogen, by forcing a positron around a nucleus containing an antiproton. However, no other antiatoms (other than antihydrogen) have been created, yet.

The subatomic particles in antimatter have an electrical charge opposite to the subatomic particles of ordinary matter (e.g. electrons, neutrinos, photons). Since these anti-subatomic particles have opposite charges (excitations) of the same quantum field, when a particle and antiparticle meet, they will ‘annihilate’ (destroy each other) and release energy in the form of gamma rays. This annihilation is exactly like how “x2 = 4” has two solutions: x = 2 or x = -2 and when they meet they annihilate.

Although matter consists of almost everything around us, antimatter is quite rare in our universe. It is believed that only about one in every 100 million particles is composed of antimatter. On the other hand, the rarity of antimatter in our universe is a good thing.

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The amount of energy we can generate by annihilations are far more significant than conventional methods which we are using today. Just one billionth of a gram of positrons has equally as much energy as 37.8 kilograms of dynamite. Einstein’s most famous equation: E = mc2, is a great way to describe where all of this energy comes from. The speed of light is an enormous number (3 × 108 ms-1), so just the smallest amount of mass can be converted into a significant amount of energy. Unfortunately, antimatter’s usefulness as an energy source is inefficient due to its enormous cost. Because each antiparticle needs to be created individually, the process of creating antimatter requires vast amounts of energy. In 1999, NASA approximated it would cost $62.5 trillion for just one gram of antihydrogen.

On the other hand, Antimatter does not have to be created in labs, although finding a reasonable amount of antimatter in nature is very rare. The most viable sources of natural antimatter would be from supernovas or solar flares. Supernovas–the explosion of stars–shoot out cosmic rays travelling at extremely high speeds. Even if just one particle in these cosmic rays happens to collide with another high-energy particle, some of the energy from the collision may be converted into forming a particle-antiparticle pair. Alternatively, Solar flares (an explosion on the surface of the sun due to magnetic field lines getting tangled) are quite frequent and are reliable sources of antimatter. During these solar flares, scientists believe that antimatter is created when high-speed particles collide with the slower particles of the Sun's atmosphere.

Antiparticles can be made in laboratories by using particle accelerators. These particle accelerators speed up particles almost to the speed of light so that two particles can be collided together with as much energy as possible. The particle accelerator works with charged particles as these particles can be accelerated by an electric field while interacting with it. The energy released from this reaction can be transformed into mass. Moreover, when energy turns to mass, both matter and antimatter are created in equal amounts. However, possibly the most renowned centre for scientific research within the field of particle physics, CERN (The European Laboratory for Particle Physics), has a different approach to creating antimatter. Scientists at CERN found out that when a significant amount of energy is forced into minimal space, particle-antiparticle pairs will spontaneously be produced. CERN conducts these experiments with high-energy particle collisions. The energy provided to the accelerated particles has to be equal to the mass of the new particles for the antiparticle-particle pairs to be created. The more energy put into the collision, the larger the particles and antiparticles will be.

Commercially, antimatter could be used for a medical technique called positron emission tomography (PET). These PET scans are most commonly used to detect cancerous tumors. During a PET scan, patients would ingest a drug containing a radioisotope that decays to produce positrons, the positron then meets its matter twin: an electron, they combine, and annihilate giving off x-rays. These x-rays are then visualized by a camera that locates where the radioisotope went so that doctors can visualize cancerous cells, as well as early signs of various disorders, such as Alzheimer’s disease and epilepsy. Additionally, CERN has a team that uses antimatter as a tool; the “Antihydrogen Experiment on Gravity, Interferometry and Spectroscopy (AEGIS)” is a project that gathers physicists from all over Europe in the aims of identifying the effect that the Earth’s gravity has on antimatter. Currently, there aren’t as many commercial applications for antiprotons. However, scientists are testing methods to use antiprotons in directly treating cancer the same way that protons are used for cancer treatment. Furthermore, research has been done to use antimatter-matter annihilations as a source of energy. When annihilation occurs, the mass of the particle and antiparticle is converted into pure energy; research is being conducted on how to harness this energy; however, creating and storing antimatter requires a lot more energy. In conclusion, antimatter is fundamentally the opposite of everyday matter. Its annihilations create vast amounts of energy and, in the future, we may be able to harness this energy. Moreover, Dirac’s discovery of antimatter is a notable one within the field of science and can possibly dictate the wellbeing of future generations.

At CERN, particle beams are used so that protons with very high levels of energy (about 26 Giga-electron volts) can collide with nuclei. When this happens, there is a possibility that proton-antiproton pairs will spontaneously be produced. If these pairs are produced, the antiproton will be separated and guided to the Antiproton Decelerator, where the antiprotons are slowed down so that they can be trapped and studied. CERN gets other antimatter particles such as antielectrons by taking radioactive salts and pulling off its decay products, antielectrons.

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Martians…? Suneh Bhatia 10F

Mars. It’s freezing, has no atmosphere, no water and is deemed uninhabitable…or so we think.

The space shuttle MAVEN was sent out by NASA to capture how exactly Mars lost its atmosphere. It concluded that due to Mars’s absence of a magnetic field there was almost nothing to protect it from the solar wind, which transports mostly particles (protons and electrons) from the sun to space at a walloping speed of 1,000,000 miles per hour. Solar wind carries a magnetic field and as it travels past Mars it forces the planet to develop an electric field, which speeds up the positively charged atoms in Mars’ upper atmosphere and then fires them into space. This eventually deteriorated the atmosphere.

The idea of extraterrestrial life existing in the universe has always been a mystery to scientists, and to think that we are the only life forms hovering around in the entire universe is a daunting thought. But as humans, if we are going to search for alien species, our best chance goes to Mars. What happened to Mars? When the solar system was formed not only did Mars have water, it also had an atmosphere to blanket and keep it warm, making it highly compatible for life to exist. For Mars to be wet and warm, it’s atmosphere must be thick and should contain carbon dioxide. Being a greenhouse gas it would’ve increased the temperatures of the planet as well as prevented the liquid water from freezing or boiling. But all this changed, Mars lost its atmosphere, its blanket of protection, and became as some might call it, a desolate wasteland. Uninhabitable.

Image captured by NASA’s Mars Reconnaissance Orbiter of ravines caused due to former lakes and rivers

Water Most astrobiologists believe that water is essential to life, and if we are going to begin our search for extraterrestrial beings we should start with water. However Mars is dry and barren, and a majority of its water lies in its frozen polar ice caps. But this does not mean that Mars is a complete stranger to water. Scientists believe that Mars wasn’t always parched and dried up, they believe that water had indeed existed in

To fully understand whether it is even possible for life to exist on Mars, we need to go back and understand what may have caused this chain of events to occur.

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streams and rivers, and that prodigious oceans once gushed through the terrains of the red planet. The first evidence for water in Mars popped up in the year 2000, where photos from NASA’s Mars Global Surveyor detected ravines formed due to the pressure of flowing water. This could prove the hypothesis that Mars used to have liquid water, making it more compatible to live in.

rocky terrain. There have been cases of 34 Martian meteorites, leading scientists to conclude that 3 of them contain evidence that point to former lifeforms that could have existed on Mars. One meteorite found in Antarctica appeared to have fossilized bacteria-like organisms, which surprisingly were not created biologically but rather volcanically. The second meteorite contained traces of fossilized nanobacteria. The third rock carried microbes, but scientists have yet to prove what caused the development of these microscopic lifeforms. Unlocking the secret to how these former life forms were created could open a huge gate to help expand our knowledge and research, and allow us to further explore the galaxy for life.

If this is true, then the likelihood of organisms existing at that time is very high due to the wide scope and sufficient volumes of water needed to survive. One of Mars’s former oceans filled up around 19% of the planet’s surface, which is just under the second largest ocean on Earth, the Atlantic Ocean, which covers about 21% of the Earth’s surface. Although we aren’t exactly sure what happened to the fundamental liquid, researchers believe that it was lost to space. This means that Mars could have been habitable for us billions of years ago, and still may be habitable for some evolved organisms.

Conclusion There may not be any life forms on Mars at the moment, but there is a great chance that there were billions of years ago. We aren’t exactly sure that there are ‘Martians’ living on Mars. Even if there were millions of years ago, is it possible that some species may have evolved to bear with the present harsh conditions on Mars? If not, is there a chance that we could be the next Martians?

Although Mars was cleared of 87% of it’s water, scientists have reasons to believe that there still may be running liquid water on the surface of the planet or beneath it. It is highly possible that there are organisms living underneath the surface of Mars, as the water underground could shield lifeforms from the severe radiation.

With the path Earth is headed, the human race doesn’t have an exactly bright future at the moment, and Mars could be our greatest chance at survival. Companies such as SpaceX and NASA have already made immense efforts to start preparing us for the red planet. With its former habitable conditions, it could be our greatest hope in sustaining the human race.

Visitors from Mars Earth has been blasted with rocks from Mars, which have been emitted from the surface of the red planet due to collisions of asteroids and comets against the

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Hyperloop: The future of transport Matthew Wright 12W

As humans, we have always been looking for ways to improve our lives and advance civilisation. One area that has constantly been changing is the way we travel. Transportation allows us to spread information and resources across the globe. So what is the next great innovation in commercial travel? The answer is the Hyperloop.

are installed at the front to suck in the compressed air and redirect it through the capsule, overcoming the Kantrowitz limit. Some of the air can be redirected to the back for additional propulsion, but most is sent to the air bearings underneath the capsule. These bearings use the air around them to create pressurized cushions of air which support the capsule, essentially levitating it rather than riding on a fixed track. The air bearings are 1.5 metre paddles that are primarily responsible for the high speeds that the capsules are capable at travelling at by reducing friction. Friction is even further reduced by having a streamlined body shape.

Tesla founder and SpaceX CEO Elon Musk proposed the Hyperloop back in 2013. It involves the principles of fluid dynamics and electromagnetism to transport passengers in a capsule called a passenger pod.

While friction is significantly reduced, it’s not eradicated entirely. Although a perfect vacuum could theoretically completely remove friction, it isn’t economically sustainable as it would have to be maintained for hundreds of miles.

The Hyperloop has been dubbed by many as the future of travel. It is planned to be self powering and unobstructive to civilisation. The main power that will be provided to the electromagnetic motors will come from solar panels installed on top of the tubes. At its core, it is a 2 track design contained in a near vacuum tunnel tube. The capsules are placed in the tube and hover inside it. The tube contains low pressure air at approximately 0.01 atmospheres - a hundredth of the air pressure at sea level. The two end of the tubes contain airlocks to sustain the low air pressure when passengers are getting in or out of the pods that is controlled by an external air pumping station.

Passenger pods are primarily propelled by electromagnetics, similar to the technology in Tesla electric cars. More specifically, linear induction motors are placed along the tube while permanent magnets are put on the pods. Together they create passive magnetic levitation due to the forces resulting from the interacting magnetic fields. The linear motors are also responsible for accelerating and decelerating the pods. These speeds mean the capsules will allow commuters to travel the 350-mile route from Los Angeles to San Francisco in just 30 minutes. The whole system has been envisioned above ground with safety plans against natural hazards. The pillars that the tubes will rest on will be able to sway in the event of an earthquake. Another unique planned feature of the tubes is that each section will be flexible in that they will curve and change shape if the terrain shifts around. The ability to do this is due to the

Even at low pressure, objects moving forward in similar tubes will push against the air in front of it, hence compressing it. This creates a cushion of air in front that slows the object down and limits its speed. Such a phenomenon is called the Kantrowitz limit. To tackle this, the Hyperloop pods have compressor fans

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passenger pods not entirely relying on a fixed track inside the tube as they are mostly levitating. A Hyperloop test track in Nevada, USA, has designed pillars to take weight 10 to 15 times more than the pods and the tube itself in order to stay resistant against earthquakes. Proposed Hyperloop ticket prices are as low as bus prices, which would be much better for most travellers due to the faster travel time. As a result, traffic on the roads would be reduced, leading to a decrease in potential for road accidents, casualties and pollution. In addition, Hyperloop capsules will be more frequent than other high-speed transportation with plans to have pods serving passengers every 30 to 120 seconds.

Currently the first cargo transport system is planned for as early as 2020, which is looking realistic based on the initial inexpensive construction value. The financial cost for the proposed 350-mile route from Los Angeles to San Francisco is set at USD$6 billion, which is much cheaper than a high speed rail network that might cost USD$70 billion over the same distance. Such an advancement in technology with these innovative designs are looking likely to pave the way for the future of transport; one that is the safest, fastest and most convenient system that the world has yet to see.

However, with such ambitious designs there are always challenges to overcome. One concern that has been raised is the temperature variation in the tube. On a hot day the high temperatures will cause the metal to expand and the length of the tube to extend. Similarly, cold temperatures would cause the tube length to contract. This is a common problem in many engineering projects that is often solved with expansion joints. For example, bridges nowadays use these joints in its structure to allow for the varying extension during temperature changes. However, this cannot be used in the Hyperloop as if they were installed in the tubes it wouldn’t keep the airtight seal that is essential for the system. A modified solution for this problem would be to place large expansion joints at the ends of the tubes instead. The joints would have to be in total 300 metres long to compensate for all the potential extension from thermal expansion. This technology is similar to airport walkway extensions to transfer passengers from the airport gate to the plane.

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Learn to Paint like Van Gogh Overnight Angie Wong 12F

Being able to draw like the master artisan in the 19th century may be farfetched for some of us, but with recent developments in technology, it may not be impossible after all. Imagine if you were given a magic wand which could transform a few simple lines into a multimillion dollar drawing. If your doodles turn out to look like child sketches, fear no more. A newly developed AI, Vincent, turns ordinary sketches into a piece of digital art. What is Vincent? The artificial intelligence (AI) system, dubbed Vincent, is a deep learning demonstration created by UK-based firm Cambridge Consultants. It is a machine that can complete a drawing from a simple human sketch. Named after the renowned artist Vincent Van Gogh, Vincent was shown around 8000 paintings from the Renaissance period, by artists such as Van Gogh, Cézanne and Picasso as well as paintings in the current era. This allowed the system to interpret the contrast, colour and texture of a specific painting.

Artificial Intelligence Artificial intelligence (AI) is the simulation of human intelligence. Artificial intelligence is a branch of computer science that aims to create intelligent machines that function like a human. However, learning without supervision requires a machine to apply what they have learnt to make decisions, which is often referred to as machine learning. The main technique used in Vincent is deep learning. Deep learning is a subset of machine learning which is a technique that allows machines to learn on their own using examples. Other uses of deep learning include driverless cars, voice control in speakers, etcetera. An easy way to differentiate between machine learning and deep learning is that machine learning requires you to tell the machine how to interpret the data and make an accurate prediction, while deep learning allows the machine to learn through its own computing. Essentially deep learning involves feeding a system with large amounts of data, and the system then moves on to make its own decisions about other data. The data is fed through neural networks, a set of algorithms modelled after the human brain in order to recognise patterns. This allows the machine to group unlabelled or unsorted data according to similar patterns with the input that was fed into the machine. Linking back to Vincent, when you draw a random shape, the machine searches through its large database of renaissance art to spot for similarities and adapts the

To use the machine, one simply draws onto a tablet with a stylus – an instrument shaped as a pen used to interact with computer screens. After the user selects one of the seven styles of artwork, Vincent interprets the lines drawn and ‘completes’ the drawing.

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old artwork into a new one. Through the input data of Vincent, it learns where colour and texture contrasts in most paintings, and therefore figures out the outlines of your sketch, making decisions on how to fill the painting in.

General Adversarial Networks (GAN) One of the technologies Cambridge Consultants used to create the AI is GANs. GANs are deep neural networks made up by two nets (the generator and the discriminator), which are put one against the other. The generator generates new data based on the information it receives while the discriminator reviews the data and determines whether it belongs in the data set. The generator’s goal will be to convince the discriminator that the generated data is real data that was inputted, and therefore forms the idea of putting one against the other. Similar Applications There had been other recent development on this area, such as Prisma, a photo editing app which turns photos and videos into pieces of art inspired by famous artists such as Van Gogh and Picasso. Prisma also uses neural networks to recreate the image using techniques that was fed into the system on a blank canvas. The app analyses the image, and recreates it while adapting the style and texture from a famous piece of art. However, what’s more special about Vincent is that it makes further decisions by filling in the incomplete aspects of the sketch, while Prisma just reinterprets the pixels in the image with an artistic style. Further Development The main point to note about the robot is that it demonstrates the power of machine learning, and that it is not just a tool to entertain the masses. This development in deep learning can be further applied to technologies such as autonomous vehicles, digital security and other areas which require the interpretation of images and data. Nonetheless, deep learning requires a huge amount of data for training, which explains why it has only been recently introduced. This proves that the training process is both time consuming and extremely technical, which requires machines with high performance Graphics Processing Units.

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T-Cell Therapy: A Cure for Cancer? Mallika Laul 12F The human immune system is the body’s defence against pathogenic diseases and infections. The immune system is comprised of many different types of cells that collectively work to destroy foreign bodies that enter the system. These cells are called white blood cells and are split into two classes: the innate immune system and the adaptive immune system. The innate immune system is the body’s second line of defence and is non-specific in its response to foreign substances. The principle component of the innate immune system are phagocytic white blood cells that essentially engulf and digest foreign bodies through a process called phagocytosis. Phagocytic leukocytes circulate in the blood stream and move into the body tissue by extravasation. The white blood cells are drawn to the tissue as these damaged tissues release chemicals such as histamine which signal the site of an infection. The pathogens are engulfed when cellular extensions called pseudopodia surround the pathogen and fuse to form an internal vesicle in the phagocyte, this fuses to a lysosome and the pathogen is digested by digestive enzymes. Pathogen fragments called antigens are then presented on the surface of the phagocyte in order to stimulate the third line of defence, involving the adaptive immune system.

release cytokines to activate the particular B cell capable of producing antibodies specific to the antigen. The B cells will then go on to divide to form temporary plasma cells that produce large amounts of the specific antibody. Cancer cells also have antigen markers present on their surface, but it is more difficult for the immune system to recognise these cells as foreign bodies. This means that not all immune cells have the right B cell receptors to recognise the cancer cell antigens and produce antibodies in response.

The adaptive immune system is specific in its response, it can differentiate between certain [picture] types of pathogens and modify its response to be specific to that type of pathogen. This process is coordinated by lymphocytic white blood cells, that produce antibodies. B cells are antibody producing cells that recognise the antigens presented on the surface of the phagocytes and produce the respective antibody in response. These antibodies or immunoglobulins are Y shaped protein molecules that bind to the antigen markers on the pathogen surfaces and make them impotent. The antibodies divided section will bind to the pathogen or damaged cell whilst the uniform end or the constant end will bind to the proteins of the outside of the white blood cells

Chimeric Antigen Receptor T-Cell Therapy: How it Works Immunotherapy is a method to fight cancer that employs the body’s immune system, to fight the disease. This basically constitutes antibodies being taken from the patients’ blood stream, reprogrammed to recognise specific proteins found in cancer cells, then reintroduced into the patient’s system. This process can take up to several weeks.

Helper T cells are regulators that release chemicals called cytokines to trigger specific B cells. The antigen presenting cells called dendritic cells migrate to the lymph nodes and activate the helper T cells, these

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A sample of T cells is taken from the blood through a process called leukapheresis. Two IV lines are connected to the patients two arms, blood is removed through one and returned through the other. This can also be done through the aid of a central venous catheter that serves the purpose of both lines. The patient will remain still for 2-3 hours during the procedure. As the blood is taken from the patient's arm it is passed through an apheresis machine, which separates the different parts of the blood. In this case

Side Effects Minority of the patients tested experienced serious side effects from this treatment, extracted as CAR T-cells multiply in the body itself. Serious side effects include cytokine release syndrome (CRS) with high fevers and extremely low blood pressure, which may occur in the first week of treatment. Another major side effect that could occur is neurotoxicity, casing seizures or severe headaches. Moreover, CAR T-cell therapy is designed to recognise and attack the protein antigen CD19 present on most B cells, meaning that they destroy healthy B cells as well as cancerous ones. This could result in the reduction of B cells or even the complete eradication of B cells within the body, weakening the immune system.

the T cells will be extracted, and the rest of the blood cells are transferred back into the patient's body through the secondary IV. These T cells are then taken to the labs in order to genetically engineer them through the addition of the specific chimeric antigen receptor (CAR), creating CAR T-cells. These CAR T-cells are designed to recognise and target a specific protein on the cancer cells. These changed T cells grow and multiply in the lab, this takes a few weeks as many CAR T-cells is needed for this method of therapy. Once there are enough cells you have a drip containing these cells back into your bloodstream. A few days before the infusion of these cells back into the bloodstream the patient may receive weak chemotherapy to lower the number of antibodies so that the CAT T-cells have a higher chance of being activated. Once the CAR Tcells start binding with cancer cells, they start to increase in number and can destroy even more cancer cells

Approved Therapies In initial trials conducted by Dr. Stephen Grupp of the Children's Hospital of Philadelphia all signs of cancer disappeared in 27 out of the 30 patients involved in the study. Furthermore, the majority of these patients expressed no signs of relapse in the long term. This success caused larger trials to form for children and adolescents with leukemia. Based on the trial results, the FDA approved CAR T-cell therapy for patients with acute lymphoblastic leukemia in August 2017. Initial trials of this type of therapy has largely surrounded blood-based cancers that develop from B

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cells such as acute lymphoblastic leukaemia and chronic lymphocytic leukemia. This research targeted proteins on the surface of the B cells called CD19. Research on this type of therapy is growing fast as the biopharmaceutical industry increases their involvement, with clinical trials expanding from just a handful 5 years ago to over 180 now. These trials are beginning to focus on proteins other than CD19 as not all patients have responded to this kind of targeted therapy, and some patients experienced a relapse of their disease. This was due to the B cells eventually no long expressing this CD19 marker, known as antigen loss. Centres began to test another antigen targeted therapy of CD22, but this resulted in similar effects. Researchers are now attempting to improve durability and perhaps at least forestall antigen loss, if not prevent it altogether, is to attack multiple antigens simultaneously. Several research groups, for example, are testing T cells that target both CD19 and CD22 in early-phase clinical trials.

What makes it different? Other traditional therapies for cancer include chemotherapy which involves the use of one or more drugs to kill cells in the body and radiation therapy which involves damage of cancer cells in a certain area. For these therapies different types of drugs are required depending on the type of cancer the patient has, and once the dosage is stopped the treatment generally stops as well. On the other hand, CAR T-cell therapy enhance the persons existing immune system in order for it to fight the cancer itself. Ultimately, CAR T-cell therapy will need to go through long periods of testing before being considered a viable and manageable therapy for all types of cancer, but as more and more trials are being conducted this could be an imminent solution.

Additionally, there is debate over whether this therapy will have the same success in solid tumors as finding suitable antigens to target solid tumours may be too difficult to a large extent. Researchers from the National Cancer Institute estimated that tumor antigens largely reside internally for tumor cells, this means that CAR T-cells would have no effect as they can only bind to cell surface antigen markers. Investigators are already conducting trials for the attack of a protein called mesothelin which exists on tumor cells in some of the worst types of cancers such as pancreatic cancers as well as the protein EGFRvIII which is present on almost all cells in patients with aggressive glioblastomas (brain tumors).

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The Beginning of Genome Editing Megan Lee 12F many genes at once and is extremely helpful when studying complex diseases that involve many genes acting together.

Every cell in our body contains a copy of our genome, containing over 20,000 genes and 3 billion letters of DNA bases. These genes make us who we are; they define us as individuals, and as a species. What would happen if we could successfully edit this? CRISPR (which stands for Clustered Regularly Interspaced Short Palindromic Repeats), invented in 2015 by Jennifer Doudna, has been dubbed as the ‘biggest biotechnology discovery of the century’ by the MIT technology review in 2016, with the potential to cure a variety of diseases. But scientists have been tinkering with genome editing for years now - what makes CRISPR so special? Simply put, this advent of precise, affordable and efficient genome editing has seen a sudden breakthrough in scientific research; from preventing hearing loss in mice to virus resistant pigs.

Diagram showing gRNA matched with the pam, and cas9 cutting the DNA strands

How does it work? The CRISPR-cas9 system is based on a natural system that bacteria utilise to protect themselves from pathogens, specifically viruses. This sophisticated ‘immune system’ they possess has been adapted by scientists, hence it can be used in other contexts. There are two molecules that mutate the DNA: cas9 and gRNA. Cas9, which stands for CRISPR associated protein 9 nuclease, is a restriction endonuclease enzyme. This means that it can cut both DNA strands at a specific location in the genome. From there, DNA can be inserted or removed. gRNA, which stands for guide RNA, is a short pre-designed RNA sequence located in a longer RNA strand. Bound together, these two molecules form a complex that searches through all DNA in the cell in order to find parts that match sequences in the gRNA. This part is called the ‘pam’, which stands for the protospacer adjacent motif. The complex binds to the pam and unwinds the double helix. If the sequence matches to the RNA, cas9 cuts the DNA twice, leading to a double-strand break. Put simply, this cas9-RNA complex can be thought of as a pair of scissors that can make a double-stranded break in the double helix. At this point, the cell attempts to repair the DNA, but this reparation process is extremely error-prone, often leading to mutations which disable the gene. As this complex is programmable, scientists can alter it to recognize certain sequences and break the DNA at a specific location. It can be used to study

Background information: DNA and RNA DNA is composed of two strands of polynucleotides, wound into a tight double helix. A polynucleotide strand is a strand of many nucleotides linked together, and a nucleotide is the building block of genetic material. It contains a phosphate group bonded to a sugar, bonded to a nitrogenous base. Diagram showing the structure of a nucleotide

There are 4 possible bases for a nucleotide (these are called Adenine, Thymine, Cytosine and Guanine), therefore there are 4 different nucleotides. RNA is very similar to DNA; however, it only has one strand, has a different sugar, and has 1 different bases (its bases are called Adenine, Uracil, Cytosine and Guanine).

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Applications CRISPR holds potential for curing a wide variety of diseases, ranging from genetic disorders such as cystic fibrosis to treating complex diseases such as cancer and HIV. For example, researchers at Stanford University are attempting to cure sickle cell anaemia by correcting the mutation in the haemoglobin gene to convert sickled red blood cells into regular ones. As aforementioned, David Liu and other researchers at the HHMI recently used CRISPR-cas9 to prevent hearing loss in mice by packaging the cas9 and gRNA complex in a greasy bundle. Although scientists have a long way to go before using this technology on humans, such a change could make a sizeable difference in the quality of life of deaf patients. Apart from treating diseases, there are many other applications of CRISPR technology. From tobacco to tomatoes, CRISPR has been applied in food and agricultural industries to enhance crops. Companies have already begun producing and selling meat that is more tender and drought-tolerant corn. What’s more, many governmental agricultural departments do not regulate CRISPR edited foods as new genes are not necessarily inserted, rather their existing genes are cut. With such open regulations, CRISPR will revolutionise the food industry - the potential benefits are limitless. Some opportunities include improving food safety by making food immune to pathogens and developing products with more desirable traits, such as improved taste and appearance.

Issues and Ethical Considerations With great power comes great responsibility, thus such an advancement in genetic modification brings a barrage of ethical questions. Scientists at Hokkaido University predict that doctors will soon have the capability to alter genes in human embryos using CRISPR. If changes are made to genes in gametes (sperm or egg cells) or embryos, these edits could be passed onto the next generation. This raises the question of the extent to which genome editing is ethically acceptable. Can we use it to enhance ordinary traits or should we only use it to treat diseases? What is the defining boundary? Furthermore, CRISPR is not 100% accurate or efficient. In a study conducted in rice by Doudna, gene editing only occurred in 50% of cells that received the complex. Moreover, other effects were observed, as the DNA was cut at sites other than the intended, leading to unplanned mutations. Hence, editing our genes raises the possibility of unknown and inadvertent consequences, due to our limited knowledge of genetics. As such, embryo genome editing is predominantly illegal.

Conclusion Ultimately, CRISPR technology holds great promise for treating complex diseases and genetic disorders. But first, further research must be conducted to enhance our knowledge of genetics. We must decide the degree to which genome editing is ethically acceptable.

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Epigenetics: Famine passed down generations Alice Zhang 12R They occur when DNA or histones (proteins that DNA wraps around) are assigned chemical labels. The organization of these chemical labels in a cell is called its ‘epigenome’, where ‘epi-’ again stands for above and ‘genome’ refers to the complete set of genetic information in a cell. Our epigenome can be influenced by environmental factors such as our diets (such as in the case of the famine) and smoking habits. Researchers previously believed that these epigenetic labels were completely erased when gametes formed but discovered that some of the epigenetic labels do in fact remain and are passed onto the next generation. In the case of the children born after the famine, they found certain epigenetic labels in their DNA that were caused by a process called methylation.

The Dutch Famine, which occurred between 1944 and 1945, was believed to be caused by a combination of war and poor agriculture. Food supplies became scarce during this period, and people were restricted to 400800 calories per day - approximately a quarter of the daily recommended intake. The famine eventually passed, and people started to have more to eat again. Looking back at the records on this famine, researchers found that babies who were born during this brief period were at a higher risk of health problems. But they also discovered something interesting: the children of these babies who survived during the famine were also underweight and had higher risks of health problems.

Methylation reduces gene expression by adding methyl groups to sections of DNA. It silences genes by interfering with transcription and causing DNA to wrap more tightly around histones, making the DNA less accessible for transcription. In the case of the famine, scientists found a lower than normal methylation of the IFG2 gene, which is important for making a protein called ‘insulin-like growth factor 2’ – one of the genes responsible for human growth and development. The lack of methylation may have been due to lack of methyl groups, which we derive from amino acids such methionine, and may have been caused by the lack of proteins and essential amino acids in people’s diets during the famine. Their explanation for this? Epigenetics. The prefix ‘epi’ means above, while ‘genetics’ refers to the study of heredity. Epigenetics is the study of changes in organisms above the level of genetics: changes that occur in the level of gene expression rather in the DNA itself. Genes, which are sections of DNA that code for proteins, are expressed in a two-step process. They are first transcribed into RNA, and then translated into proteins by ribosomes. These proteins produced are responsible for the cell’s characteristics. Epigenetic changes affect the transcription part of this process and can promote or inactivate the transcription of certain genes, leading to varied levels of gene expression.

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Implications of Epigenetics: Cancer Epigenetics is very important for the function of cells: it plays a role in cell regulation, cell differentiation and the cell cycle. However, unintended epigenetic changes can lead to cancer. For example, if a gene that makes a tumor suppressing protein were to be silenced, cells would be at risk of becoming tumors. On the other hand, higher than normal expressions of a gene may lead to excessive protein production and uncontrolled growth.

DNA methyltransferases, which methylate DNA, are also targets for cancer research. Many cancers have excessive methylation in the promoter regions of DNA, lowering transcription activity of genes such as tumor suppressor genes. DNMT inhibitors could help reverse these harmful changes by reactivating the genes responsible for making tumor suppressing proteins and getting rid of cancer cells. In fact, two DNMT inhibitors have already been approved by the FDA to treat myelodysplastic syndromes (a group of cancers in which cells in the bone marrow are damaged): 5Azacytidine and decitabine.

The cases above show that cancers can form due to both the hypermethylation and hypomethylation of DNA. Too much methylation means that a certain gene may not be expressed enough, while too little methylation means that a gene may be expressed more than needed – both of which can lead to cancers (as illustrated in the diagram below). Lung cancer samples, for example, were found by researchers to contain more than 80 hypermethylated genes. Scientists are currently researching the applications of epigenetics to treat cancers. One thing that stands out about epigenetic changes is that unlike DNA mutations, epigenetic changes are not entirely irreversible – which makes changes easier to reverse. Drugs are currently being developed to block the silencing of tumor suppressing genes caused by changes in gene expression. There are two enzymes that are especially important to research: histone deacetylases (HDACs) and DNA methyltransferases (DNMTS). HDACs balance with another group of enzymes called histone acetyltransferases (HATs) to regulate the balance between histone acetylation (the addition of an acetyl group, CH3CO) and deacetylation. HDACs remove acetyl groups, causing DNA to be wrapped more tightly around the histones and making it less accessible for transcription (leading to less gene expression). Mutations in the genes that code for HDADs have been known to form tumors, so researchers are currently studying methods of creating HDAC inhibitors. These inhibitors would fix levels of acetylation so the genes that have previously been wrapped around the histones too tightly would be loosened up, allowing for the ‘right’ amount of transcription to take place.

Conclusion Although the application of epigenetics to treat cancer is still at an early phase, there is a lot of hope for this type of treatment to provide an alternative to the more invasive chemotherapy and be available to treat a wide range of cancers in the future.

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Role of Bone hormone in glucose production Miyu Terashima 12N Hormones are the body’s chemical messengers that travel through the bloodstream to stimulate specific cells or tissues into action for regulation. You may have heard this term in biology, where teachers may have taught you that hormones are produced by your endocrine glands or organs which are then carried to the bloodstream. However, there is a hormone that is produced only from the human bones and not from any other endocrine glands. This hormone is called Osteocalcin, and it is a complete new type of hormone that is currently being spotlighted from scientists all over the globe. The Osteocalcin hormone is mainly released when the bones are stimulated so that they are delivered to all the different organs in the body for activation. Osteocalcin contributes to the regulation of glucose metabolism. It is important to control levels of glucose in our body because glucose levels that run out of control could lead to serious short-term problems such as hypoglycemia (deficiency of glucose) and hyperglycemia (excessive blood glucose levels). Long term problems could involve damaging vessels that supply blood to organs, meaning that organs in our body cannot retrieve substances that are needed for proper function efficiently from the blood or to remove any toxic waste. Blood glucose levels are regulated by two opposing hormones, insulin and glucagon. Insulin is secreted by the pancreas in response to elevated blood glucose levels, for example after eating a meal so that glucose levels don’t rise too much. Glucagon is released from the pancreas, so more glucose can be produced in cases of low glucose levels. Although it may seem as if only insulin and glucagon are involved, Osteocalcin has the main responsibility to stimulate the two hormones, so they activate under certain conditions. It can directly stimulate more insulin production for release to increase glucose levels in the blood, or indirectly stimulate glucagon-like-peptides to be secreted in the small intestine. These two functions of Osteocalcin enhance insulin sensitivity in the muscle.

Osteocalcin have gained the attention of scientists in the most recent years. Investigation in Osteocalcin was considered an unexpected development of bone biology, as it is now known that the bone can act as an endocrine organ and can help with controlling numerous processes in the body. Although biologically Osteocalcin is a protein, Osteocalcin is considered as a hormone because of its ability to regulate processes. A lot of Osteocalcin are available within the bones and can currently only be made by cells that form the new bones in the body called Osteoblasts. These Osteoblasts are found on the surface of the new bone, and they control calcium and mineral removal. Your bones are constantly forming and breaking down, where the build-up of your bones is influenced by a variety of vitamins. Osteoblasts usually release Osteocalcin to produce new bones, but this hormone actually is responsible for another greater role of the body.

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This particular function of Osteocalcin indicates that there is a high possibility of curing diabetes using a more efficient method. As mentioned earlier, high blood glucose levels need to be regulated or else hyperglycemia may occur. This is a hallmark sign for both type one and two diabetes, and scientists are currently investigating how Osteocalcin can be an important factor linking between bone and glucose regulation in the blood. “Studies have shown that, for some people, changes in blood concentrations of Osteocalcin may even stave off the development of diabetes.� says Professor Mathieu Ferron, a member of the Montreal Clinical Research Institute and other coauthors have been investigating the useful functions of osteocalcin. Studies done by the Karsenty group concluded from experiments that using mice that are deficient in osteocalcin resulted to be hyperglycemic, having accumulated body fat in their bodies with a drastic impairment in their glucose metabolism. There are several implications from this basic research some of which have been observed in humans as well. This means that there is definite evidence of Osteocalcin playing a role in glucose metabolism, meaning in the future higher glucose blood levels can be regulated if Osteocalcin is injected into the bloodstream. The results may open the door to new ways of preventing type two diabetes as well as obesity. Osteocalcin naturally declines in human as we age; women start at age 30, while men start at the age 50. So how can Osteocalcin be stimulated to be produced more in our daily lives and prevent certain diseases? Interestingly, it is just as simple as raising your calves and dropping them lightly to the ground. Doctors suggest that by spending just a few minutes every day to do some exercise or a small activity like this, you can allow more Osteocalcin to be stimulated. This will help individuals of any age to be able to prevent excessive or deficient glucose blood levels in the body. Other than its role in glucose metabolism, Osteocalcin can also help with regulation of calcium in the bone, increasing neurotransmitter production in the brain or even with reducing risks to get a bone fracture. Scientists are continuing to investigate any other roles of Osteocalcin and how it can benefit our bodies.

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Martians…?

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Hyperloop: The future of transport

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The Beginning of Genome Editing

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Is science journal 2017 - 18  

Island School Science Journal 2017-2018 Articles written by students

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