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Interaction Site Evolution
Interaction Site Evolution

... COMPUTER SCIENCE - Interaction Site Evolution DNA is the blueprint for generating strings of amino acids which fold into proteins. The interactions these proteins form with each other are primary components of organismal physiology. Proteins assume very specific shapes, and the amino acids on their ...
ProteinChipâ technology is one of the most exciting advancements
ProteinChipâ technology is one of the most exciting advancements

... ProteinChip technology is one of the most exciting advancements in protein analysis in the last 5 years. The Protein Biology SystemTM (PBS) combines the power of mass analysis with chromatography surfaces on an integrated platform. The PBS can easily be used by biologists, biochemists, and clinicia ...
Capturing denaturing proteins * Small Heat Shock Protein substrate
Capturing denaturing proteins * Small Heat Shock Protein substrate

... Elizabeth Vierling and Indu Santhanagopalan Protein aggregation resulting from stress, disease or mutation poses a major threat to all cells. The ubiquitous small heat shock proteins (sHSPs) act as molecular chaperones to prevent irreversible protein aggregation and are significant components of the ...
Protein interactions are essential for many biological functions to occur. ... Erika Lacy:  Cell Biology & Neuroscience
Protein interactions are essential for many biological functions to occur. ... Erika Lacy: Cell Biology & Neuroscience

... Protein interactions are essential for many biological functions to occur. Bimolecular Fluorescence Complementation (BiFC) assay is a complementation-based technique used to study protein interactions. One benefit of this approach is that protein interactions as well as the location of that interact ...
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Bimolecular fluorescence complementation



Bimolecular fluorescence complementation (also known as BiFC) is a technology typically used to validate protein interactions. It is based on the association of fluorescent protein fragments that are attached to components of the same macromolecular complex. Proteins that are postulated to interact are fused to unfolded complementary fragments of a fluorescent reporter protein and expressed in live cells. Interaction of these proteins will bring the fluorescent fragments within proximity, allowing the reporter protein to reform in its native three-dimensional structure and emit its fluorescent signal. This fluorescent signal can be detected and located within the cell using an inverted fluorescence microscope that allows imaging of fluorescence in cells. In addition, the intensity of the fluorescence emitted is proportional to the strength of the interaction, with stronger levels of fluorescence indicating close or direct interactions and lower fluorescence levels suggesting interaction within a complex. Therefore, through the visualisation and analysis of the intensity and distribution of fluorescence in these cells, one can identify both the location and interaction partners of proteins of interest.
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