Copyright: © 2012 Davydov DR. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Increasing interest of researchers to the use of high hydrostatic pressure has marked recent trends in structural biology [1-4]. It became clear that, along with the exploration of the effects of temperature, the use of pressure as a variable parameter is indispensable for detailed understanding of the mechanisms of protein-protein interactions, protein folding and conformational transitions.
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Dmitri R. Davydov (2012) studied this question.
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