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Updated: Aug 9, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Effect of amino acid substitutions on conformational stability of a protein
Abstract:
This paper reviews studies on thermostable proteins from thermophilic bacteria and on mutant proteins of human hemoglobin, tryptophan synthase alpha-subunit of E. coli, T4 phage lysozyme, and phage lambda repressor with respect to the role of the constituting amino acid residues in stabilization of conformation. The stability of a protein is easily affected by single amino acid substitutions, by which the protein undergoes change(s) of one or more of the following: a hydrogen bond, a salt bridge, a hydrophobic interaction, the volume of the residue, a disulfide bond, or the relative position of two aromatic rings.
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