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 …

The question of whether multiple mutations within a protein sum additively or nonadditively
has fascinated investigators for more than a decade, both because of the potential …

The quantitative effect of a second mutation on a mutant enzyme may be antagonistic,
absent, partially additive, additive, or synergistic with respect to the first mutation. Depending …

The study of protein stability is changing dramatically. In the last decade, improvements in
genetic and biophysical methods have facilitated measure ments of the stabilizing …

Eleven amino acid positions in the helix-turn-helix of lambda repressor have been
mutagenized by using a combinatorial method in which alanine is substituted at each …

Department of Chemistry, Imperial College of Science and Technology, London SW7 2AY,
UK Received June 15, 1987; Revised Manuscript Received October 1, 1987 abstract: The …

Recently, a number of methods have been proposed that are designed to extract
contributions to the change in free energy associated with a given perturbation or mutation …

It is difficult to overstate the importance of proteinprotein interactions in biological processes.
Some of these interactions and their roles are well known, for instance, the formation of …

The fundamental relationship between structure and function has served to guide
investigations into the workings of living systems at all levels-from the whole organism to …

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