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Protein Interaction

Proteinâ€“protein interactions (PPIs) are the physical contacts of high specificity established between two or more protein molecules as a result of biochemical events steered by interactions that include electrostatic forces, hydrogen bonding and the hydrophobic effect. Many are physical contacts with molecular associations between chains that occur in a cell or in a living organism in a specific biomolecular context.

Protein Interaction

Quite a lot of proteins do not fight alone when they perform their functions. Proteins form complexes through protein interactions and then work. In the process of work, proteins can also change the complex of proteins by changing the function of protein complex. Therefore, studying protein interaction has become one of the most important links in studying protein function and mechanism.

Force of protein interaction

The essence of protein interaction is actually three kinds of force, hydrogen bond, intermolecular force (van der Waals force) and hydrophobic force, covalent interaction is the strongest association force, formed by disulfide bond or electron sharing. Although these interactions are rare, they are decisive in certain post-translational modifications (such as ubiquitination and SUMOylation). Non-covalent bonds are usually established through a combination of weak bonds (such as hydrogen bonds, ionic interactions, van der Waals forces, or hydrophobic bonds) during transient interactions.

Biological effects of protein–protein interactions

The result of two or more proteins that interact with a specific functional objective can be demonstrated in several different ways. The measurable effects of protein interactions have been outlined as follows:  Alter the kinetic properties of enzymes, which may be the result of subtle changes in substrate binding or allosteric effects.  Allow for substrate channeling by moving a substrate between domains or subunits, resulting ultimately in an intended end product.  Create a new binding site, typically for small effector molecules.  Inactivate or destroy a protein.  Change the specificity of a protein for its substrate through the interaction with different binding partners, e.g., demonstrate a new function that neither protein can exhibit alone.  Serve a regulatory role in either an upstream or a downstream event.

Protein Interaction Service

As a leader specialized in protein interaction analysis, Creative BioMart has acquired much experience and expert knowledge in protein interaction study. Whether you work in basic, pharmaceutical, cosmetic or agrobiotech research, we provide you with cutting-edge techniques to study protein interaction. Our customerdedicated organization allows our passionate scientists to share scientific expertise with thousands of customers all over the world.

Protein Interaction Service

Yeast two-hybrid: Genome-wide screening of protein interactions by coexpression of bait with protein libraries. Membrane-based yeast two-hybrid: Based on the split-ubiquitin protein complementation assay and detects protein interactions directly at the membrane. Mammalian two-hybrid: Allows rapid and convenient analysis of protein-protein interactions in transfected mammalian cells. Phage display technology: Obtain optimal protein binding by immobilization of an antigen on magnetic beads, and screening against a phage display library. Surface plasmon resonance (SPR): The versatile label-free BIACORE technique allows detecting and monitoring of interactions in real time. Protein array: This technique is a high-throughput method used to track the interactions and activities of proteins, and determining function on a large scale.

Protein Interaction Service

Pull-downs: Confirm the existence of a protein-protein interaction predicted by other research techniques and identify previously unknown protein-protein interactions as an initial screening assay.

Protein Interaction Service

Bio-layer interferometry (BLI): Quantitative and qualitative characterization of biomolecule interactions. CLIP-Seq technology: RNA-binding landscape mapping of interacting proteins or RNA modification sites on a genome-wide scale. Fluorescence resonance energy transfer (FRET): Test the direct interaction in vitro of two candidate proteins, suitable for both wild type and mutant proteins. Biomolecular fluorescence complementation (BiFC): This technique is based on the principle that two nonfluorescent fragments of a fluorescent protein dissected at appropriate site are brought together and reconstructed to fluorescence, depending on the association or interaction between the protein fused to each fragment. Far-western blotting: This method employs non-antibody proteins to probe the protein(s) of interest on the blot.

Benefits of working with us:

•Thorough expertise in proteinprotein interactions

•Flexible offer adapted to your requirement

•High-value scientific assistance

•Highly sensitive homogeneous assay

We will be glad to discuss details of intended interaction studies with you and develop experimental strategies/methods tailored to your requirement. Please get in contact with Creative BioMart for more information or a detailed discussion.

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