STRUCTURAL AND GENETIC-ANALYSIS OF PROTEIN-FOLDING AND STABILITY

Some proteins are very tolerant to amino acid substitution, not only o n the surface but within the core. Proteins can, however, respond very differently to the same type of replacement in different parts of the molecule. From the knowledge of these structural responses, it is bec oming possible to understand in detail the factors that stabilize prot eins, which include, for example, the hydrophobic effect, electrostati c interactions and helix-dipole interactions.