Bimolecular rate constants for formation of successively more constrained protein-protein complexed states N

Range Table - link M^-1×sec^-1
Organism Generic
Reference Northrup SH, Erickson HP. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. Proc Natl Acad Sci U S A. 1992 Apr 15 89(8):3338-42. p.3340 table 1PubMed ID1565624
Method Abstract: "In the present study, the Brownian dynamics simulation method is used to compute the rate of association of neutral spherical model proteins with the stated docking criteria."
Comments P. 3340 left column 3rd paragraph: "Pathway and Rates for Forming the Protein-Protein Bond. The formation of a fully orientation-specific complex of two protein subunits can be viewed as a stepwise process, in which the proteins initially encounter in an orientationally nonspecifc fashion, followed by rotational motions that lead to formation of an increasing number of contacts (N = 1, 2, and 3). The intermediate states are described below, and the estimated rate constants of achieving these states are given in Table 1." BD=Brownian Dynamics
Entered by Uri M
ID 112542