Abstract
The chapter reviews the results obtained from measurements of hydrogen exchange (H–H, H–D, and H–T) in proteins and related compounds. The slowness of the rate of hydrogen exchange in a protein, relative to the exchange rate observed with simple peptides under the same experimental conditions is closely related to the conformation of the protein molecule in aqueous solution. Quantitative measurements of the rate of hydrogen exchange in a given protein, under specified experimental conditions, provide a multiparameter characterization of the protein conformation (or distribution of conformations) present under these conditions. Moreover, the chapter discusses the experimental techniques that have been used to measure quantitatively the rate of hydrogen exchange. The chapter also discusses arguments that support case, as the mechanism of exchange of the slowly exchanging hydrogen atoms.
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