Rapid, electrostatically assisted association of proteins
G Schreiber, AR Fersht - Nature structural biology, 1996 - nature.com
Nature structural biology, 1996•nature.com
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 …
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 …
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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