At the molecular level, high-pressure perturbation is of particular interest for biological studies as it allows trapping conformational substates. Moreover, within the context of high-pressure adaptation of deep-sea organisms, it allows to decipher the molecular determinants of piezophily. To provide an accurate description of structural changes produced by pressure in a macromolecular system, developments have been made to adapt macromolecular crystallography to highpressure studies. The present chapter is an overview of results obtained so far using high-pressure macromolecular techniques, from nucleic acids to virus capsid through monomeric as well as multimeric proteins.
CITATION STYLE
Dhaussy, A. C., & Girard, E. (2015). Functional sub-states by high-pressure macromolecular crystallography. Sub-Cellular Biochemistry, 72, 215–235. https://doi.org/10.1007/978-94-017-9918-8_11
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