Rapid, electrostatically assisted association of proteins.
The rapid association of barnase and its intracellular inhibitor barstar has been analysed from the effects of mutagenesis and electrostatic screening. A basal association rate constant of 10(5) M(-1) s(-1) is increased to over 5 x 10(9) M(-1) s(-1) by electrostatic forces. The association between the oppositely charged proteins proceeds through the rate-determining formation of an early, weakly specific complex, which is dominated by long-range electrostatic interactions, followed by precise docking to form the high affinity complex. This mode of binding is likely to be used widely in nature to increase association rate constants between molecules and its principles may be used for protein design.
Schreiber
G
G
Cambridge Centre for Protein Engineering, Medical Research Council Centre, UK.
Fersht
A R
AR
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D004560:Electricity; D004791:Enzyme Inhibitors / Q000378:metabolism*; D008956:Models, Chemical; D008958:Models, Molecular; D009154:Mutation; D009994:Osmolar Concentration; D011485:Protein Binding; D012260:Ribonucleases / Q000235:genetics / Q000378:metabolism*; D013997:Time Factors
D001426:Bacterial Proteins; D004791:Enzyme Inhibitors; C057438:barstar protein, Bacillus amyloliquefaciens; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease