Fundamentals of protein stability
Protein stability is quantitatively described by the standard Gibbs energy change, AG:, involved in unfolding the unique, three dimensional structure to randomly coiled polypeptide chains. However, for construction of new proteins or improving stability of existing proteins knowledge of the overall AG: is not sufficient. Rather it is desirable to have parameters at hand that permit estimates of the various contributions to stability of individual interactions resulting from amino acid replacements. This presentation refers to some basic experiments and summarizes the present picture of principal forces governing protein stability.