Modeling protein association mechanisms and kinetics
Abstract
Substantial advances have been made in modeling protein association mechanisms and in calculating association rate constants (ka). We now have a clear understanding of the physical factors underlying the wide range of experimental ka values. Half of the association problem, where ka is limited by diffusion, is perhaps solved, and for the other half, where conformational changes become rate-limiting, a number of promising methods are being developed for ka calculations. Notably, the binding kinetics of disordered proteins are receiving growing attention, with 'dock-and-coalesce' emerging as a general mechanism. Progress too has been made in the modeling of protein association kinetics under conditions mimicking the heterogeneous, crowded environments of cells, an endeavor that should ultimately lead to a better understanding of cellular functions.
Journal details
Volume 23
Issue number 6
Pages 887-893
Publication date
Full text links
Publisher website (DOI) 10.1016/j.sbi.2013.06.014
Europe PubMed Central 23850142
Pubmed 23850142
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