Article
Thermodynamic and structural consequences of changing a sulfur atom to a methylene group in the M13Nle mutation in ribonuclease-S.
Biochemistry - 19 Jul 1994
Thomson J, Ratnaparkhi G S, Varadarajan R, Sturtevant J M, Richards F M
Abstract excerpt
Two fragments of pancreatic ribonuclease A, a truncated version of S-peptide (residues 1-15) and S-protein (residues 21-124), combine to give a catalytically active complex. We have substituted the wild-type residue at position 13, methionine (Met), with norleucine (Nle), where the only covalent change is the replacement of the sulfur atom with a methylene group. The thermodynamic parameters associated with the...
Topics
- Calorimetry
- Crystallization
- Crystallography, X-Ray
- Methylation
- Molecular Structure
- Mutation
- Norleucine
- Protein Conformation
- Ribonucleases
- Structure-Activity Relationship
- Sulfur