The M32L substitution of staphylococcal nuclease: Disagreement between theoretical prediction and experimental protein stability
by Spencer, Daniel S.; Stites, Wesley E.
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.
- Journal
- Journal of Molecular Biology
- Volume
- 257
- Issue
- 3
- Year
- 1996
- Start Page
- 497-499
- URL
- https://dx.doi.org/10.1006/jmbi.1996.0180
- ISBN/ISSN
- 1089-8638; 0022-2836
- DOI
- 10.1006/jmbi.1996.0180