title: Functional Sub-states by High-pressure Macromolecular Crystallography.
abstract: 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 high-pressure 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.
authors.affiliation: CRISMAT, ENSICAEN, 6 Boulevard du Marechal Juin, F-14000, Caen, France.
authors.forename: Anne-Claire
authors.initials: AC
authors.lastname: Dhaussy
authors.forename: Eric
authors.initials: E
authors.lastname: Girard
mesh_terms: D003461:Crystallography / Q000379:methods*; D006874:Hydrostatic Pressure; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins