Department of Pharmaceutical Chemistry, University of California, San Francisco, California
94143-1204 Received April 3, 1990; Revised Manuscript Received May 2, 1990 e purpose …

Recombinant DNA technology has now made it possible to produce proteins for
pharmaceutical applications. Consequently, proteins produced via biotechnology now …

The inverse protein folding problem, the problem of finding which amino acid sequences
fold into a known three-dimensional (3D) structure, can be effectively attacked by finding …

We have analysed the frequency with which potential hydrogen bond donors and acceptors
are satisfied in protein molecules. There are a small percentage of nitrogen or oxygen atoms …

A strategy, called alanine-scanning mutagenesis, was used to identify specific side chains in
human growth hormone (hGH) that strongly modulate binding to the hGH receptor cloned …

Revised Manuscript Received May 29, 1990 e energetics of virtually all binding functions in
proteins is the culmination of a set of molecular interactions. For example, removal of a …

Publisher Summary This chapter summarizes the experimental information on protein
energetics. This field is developing fast and the concept of the energetics of protein structure …

Helix‐capping motifs are specific patterns of hydrogen bonding and hydrophobic
interactions found at or near the ends of helices in both proteins and peptides. In an α‐helix …

Proteins, due to the delicate balance of stabilizing and destabilizing interactions, are only
marginally stable. Adaptation to extreme environments tends to shift the 'mesophilic' …

There is tremendous variability in the importance of individual amino acids in protein
sequences. On the one hand, nonconservative residue substitutions can be tolerated with …