Effect of amino acid substitutions on conformational stability of a protein.
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.
D000595:Amino Acid Sequence; D001426:Bacterial Proteins; D006455:Hemoglobins, Abnormal; D006358:Hot Temperature; D006801:Humans; D009113:Muramidase / Q000235:genetics; D009154:Mutation; D011487:Protein Conformation; D011489:Protein Denaturation; D012097:Repressor Proteins / Q000235:genetics; D013816:Thermodynamics; D014367:Tryptophan Synthase / Q000235:genetics
D001426:Bacterial Proteins; D006455:Hemoglobins, Abnormal; D012097:Repressor Proteins; D009113:Muramidase; D014367:Tryptophan Synthase