Protein-protein bond formation bimolecular rate constant

Range ~10^6 (0.5×10^6 - 5.0×10^6) 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. abstract, p.3338 left column bottom paragraph & p.3338 right column top paragraphPubMed ID1565624
Comments Abstract: "Protein-protein bond formations, such as antibody-antigen complexation or aggregation of protein monomers into dimers and larger aggregates, occur with bimolecular rate constants on the order of 10^6 M^-1×s^-1, which is only 3 orders of magnitude slower than the diffusion-limited Smoluchowski rate." P.3338 left column bottom paragraph: "The association of protein molecules to form dimers or larger complexes is characterized by second-order rate constants that are typically in the range 0.5-5 × 10^6×M^-1×s^-1." P.3338 right column top paragraph: "Since rates of k2 = 0.5-5 × 10^6 M^-1×s^-1 are achieved by many protein associations, including the very general reaction of antibodies with protein antigen, this range appears to represent the typical rate for proteins associating and docking at the precise orientation for bond formation, without any special steering forces."
Entered by Uri M
ID 112534