protein interaction - technology networks
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Protein Interaction
Creative Biomart. Inc.
Protein–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.
Protein Interaction
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 proteininteraction analysis, Creative BioMarthas acquired much experience and expertknowledge in protein interaction study.Whether you work in basic,pharmaceutical, cosmetic or agro-biotech research, we provide you withcutting-edge techniques to studyprotein interaction. Our customer-dedicated organization allows ourpassionate scientists to sharescientific expertise with thousands ofcustomers all over the world.
Yeast two-hybrid: Genome-wide screening of protein interactions by co-expression of bait with protein libraries.Membrane-based yeast two-hybrid: Based on the split-ubiquitin proteincomplementation assay and detects protein interactions directly at themembrane.Mammalian two-hybrid: Allows rapid and convenient analysis of protein-proteininteractions in transfected mammalian cells.Phage display technology: Obtain optimal protein binding by immobilization ofan antigen on magnetic beads, and screening against a phage display library.Surface plasmon resonance (SPR): The versatile label-free BIACORE techniqueallows detecting and monitoring of interactions in real time.Protein array: This technique is a high-throughput method used to track theinteractions and activities of proteins, and determining function on a largescale.
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.
Protein Interaction Service
Benefits of working with us:
•Thorough expertise in protein-protein 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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www.creativebiomart.net