The M32L substitution of staphylococcal nuclease: disagreement between theoretical prediction and experimental protein stability.


Abstract

The M32L substitution mutation of staphylococcal nuclease was made to test the theoretical prediction by Yamaotsu, Moriguchi and Hirono that it would be approximately 1.6 kcal/mol more stable than the wild-type protein. Instead M32L and the closely related M32I mutant were 0.8 and 0.6 kcal/mol less stable than the wild-type protein, respectively. The theoretical treatment had successfully predicted the stability effects of other mutations in staphylococcal nuclease. The discrepancy found here may be due to a general problem of the theoretical treatment, such as inadequate molecular dynamics simulation time, or possibly due to more specific difficulty in assessing the strength of the sulfur-aromatic interaction that is present in the wild-type. Study holds ProTherm entries: 7781, 7782, 7783, 7784, 7785, 7786 Extra Details: protein folding; denaturation;,sulfur-aromatic interactions; mutation

Submission Details

ID: vCMLPYcB4

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:34 p.m.

Version: 1

Publication Details
Spencer DS;Stites WE,J. Mol. Biol. (1996) The M32L substitution of staphylococcal nuclease: disagreement between theoretical prediction and experimental protein stability. PMID:8648619
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