Quantitative functional analysis of protein complexes on surfaces.
A major challenge in cell and molecular physiology research is to understand the mechanisms of biological processes in terms of the interactions, activities and regulation of the underlying proteins. Functional and mechanistic analyses of the large number of proteins that participate in the regulation of cellular processes will require new approaches and techniques for high throughput and multiplexed functional analyses of protein interactions, protein conformational dynamics and protein activity. In this review we focus on the development and application of proteomics and associated technologies for quantitative functional analysis of proteins and their complexes that include: (1) the application of surface plasmon resonance (SPR) imaging for multiplexed, label-free analyses of protein interactions, binding constants for biomolecular interactions and protein activities; and (2) high content analysis of protein motions within functional multiprotein complexes.
Lee
Hye Jin
HJ
Department of Physiology, University of Wisconsin-Madison, WI 53706, USA.
Yan
Yuling
Y
Marriott
Gerard
G
Corn
Robert M
RM
D000818:Animals; D018604:Epitope Mapping / Q000379:methods; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D020869:Gene Expression Profiling / Q000379:methods; D006801:Humans; D040081:Protein Array Analysis / Q000379:methods*; D025941:Protein Interaction Mapping / Q000379:methods*; D011506:Proteins / Q000032:analysis / Q000737:chemistry* / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D021281:Quantitative Structure-Activity Relationship; D020349:Surface Plasmon Resonance / Q000379:methods*
D011506:Proteins