The M32L substitution of staphylococcal nuclease: disagreement between theoretical prediction and experimental protein stability.
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.
Spencer
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Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, 72701-1201, USA.
Stites
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D004795:Enzyme Stability / Q000235:genetics; D008836:Micrococcal Nuclease / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D017510:Protein Folding
D008836:Micrococcal Nuclease