Mutations and the conformational stability of globular proteins.
The elucidation of the three-dimensional structure of now over 100 proteins provides the basis for describing the nature of interactions stabilizing native protein structure. To understand the forces responsible for maintaining the native structure, it is necessary to analyze the contributions of the specific forces like a hydrogen bond, a salt bridge or a hydrophobic interaction to the overall stability of a protein. Using mutant proteins carrying a single amino acid substitution, specific interactions in a protein can be altered and the effect can be studied. In this paper the results of such studies on stability variants of human haemoglobin and of T4 phage lysozyme are described.
D001419:Bacteria / Q000235:genetics; D004355:Drug Stability; D014644:Genetic Variation; D006454:Hemoglobins / Q000235:genetics; D006358:Hot Temperature; D006801:Humans; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D011506:Proteins / Q000235:genetics*
D006454:Hemoglobins; D011506:Proteins