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Automated prediction of protein association rate constants.


ABSTRACT: The association rate constants (k(a)) of proteins with other proteins or other macromolecular targets are a fundamental biophysical property. Observed rate constants span over ten orders of magnitude, from 1 to 10(10) M(-1)s(-1). Protein association can be rate limited either by the diffusional approach of the subunits to form a transient complex, with near-native separation and orientation but without short-range native interactions, or by the subsequent conformational rearrangement to form the native complex. Our transient-complex theory showed promise in predicting k(a) in the diffusion-limited regime. Here, we develop it into a web server called TransComp (http://pipe.sc.fsu.edu/transcomp/) and report on the server's accuracy and robustness based on applications to over 100 protein complexes. We expect this server to be a valuable tool for systems biology applications and for kinetic characterization of protein-protein and protein-nucleic acid association in general.

SUBMITTER: Qin S 

PROVIDER: S-EPMC3240845 | biostudies-literature | 2011 Dec

REPOSITORIES: biostudies-literature

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Automated prediction of protein association rate constants.

Qin Sanbo S   Pang Xiaodong X   Zhou Huan-Xiang HX  

Structure (London, England : 1993) 20111201 12


The association rate constants (k(a)) of proteins with other proteins or other macromolecular targets are a fundamental biophysical property. Observed rate constants span over ten orders of magnitude, from 1 to 10(10) M(-1)s(-1). Protein association can be rate limited either by the diffusional approach of the subunits to form a transient complex, with near-native separation and orientation but without short-range native interactions, or by the subsequent conformational rearrangement to form the  ...[more]

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