title: 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.
authors.affiliation: Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville, 72701-1201, USA.
authors.forename: D S
authors.initials: DS
authors.lastname: Spencer
authors.forename: W E
authors.initials: WE
authors.lastname: Stites
mesh_terms: D004795:Enzyme Stability / Q000235:genetics; D008836:Micrococcal Nuclease / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D017510:Protein Folding
chemical_list: D008836:Micrococcal Nuclease