Long-range, small magnitude nonadditivity of mutational effects in proteins

Biochemistry. 1995 Mar 14;34(10):3133-9. doi: 10.1021/bi00010a001.
No abstract available

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Glutathione Reductase / chemistry
  • Glutathione Reductase / genetics
  • Glutathione Reductase / physiology
  • Hemoglobins / chemistry
  • Hemoglobins / genetics
  • Hemoglobins / physiology
  • Humans
  • Micrococcal Nuclease / chemistry
  • Micrococcal Nuclease / genetics
  • Micrococcal Nuclease / physiology
  • Models, Chemical
  • Muramidase / chemistry
  • Muramidase / genetics
  • Muramidase / physiology
  • Mutation*
  • Protein Conformation
  • Protein Folding
  • Proteins / chemistry*
  • Proteins / genetics*
  • Proteins / physiology
  • Subtilisins / chemistry
  • Subtilisins / genetics
  • Subtilisins / physiology
  • Thermodynamics
  • Tyrosine-tRNA Ligase / chemistry
  • Tyrosine-tRNA Ligase / genetics
  • Tyrosine-tRNA Ligase / physiology

Substances

  • Hemoglobins
  • Proteins
  • Glutathione Reductase
  • Micrococcal Nuclease
  • Muramidase
  • Subtilisins
  • Tyrosine-tRNA Ligase