Abstract
A kinetic study of the hydrogen exchange reaction of a protein or a nucleic acid can provide useful information on the structure and fluctuation of such a biological macromolecule. However, reactions faster than 10s are not easily traced by the methods used in earlier studies. Recent introduction of stopped-flow ultraviolet absorption and emission spectrophotometry into the hydrogen exchange studies of proteins and nucleic acids promises great development in this field. By this new technique we can now explore the millisecond region of the time-scale of hydrogen exchange kinetics. In this discussion we demonstrate some new aspects of the dynamic properties of proteins and nucleic acids on the basis of our results obtained by the stopped flow hydrogen exchange method.
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