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Rapid, electrostatically assisted association of proteins

Nature Structural Biology volume 3, pages 427–431 (1996)Cite this article

Abstract

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 105 M−1 s−1 is increased to over 5×109 M−1s−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.

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Author notes

  1. Gideon Schreiber

    Present address: Department of Biochemistry, Weizmann Institute of Science, Rehovot, 76100, Israel

Authors and Affiliations

  1. Cambridge Centre for Protein Engineering, Medical Research Council Centre, Hills Road, Cambridge, CB2 2QH, UK

    Gideon Schreiber & Alan R. Fersht

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  1. Gideon Schreiber
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  2. Alan R. Fersht
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Schreiber, G., Fersht, A. Rapid, electrostatically assisted association of proteins. Nat Struct Mol Biol 3, 427–431 (1996). https://doi.org/10.1038/nsb0596-427

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