title: High-pressure macromolecular crystallography and NMR: status, achievements and prospects.
abstract: Biomacromolecules are thermodynamic entities that exist in general as an equilibrium mixture of the basic folded state and various higher-energy substates including all functionally relevant ones. Under physiological conditions, however, the higher-energy substates are usually undetectable on spectroscopy, as their equilibrium populations are extremely low. Hydrostatic pressure gives a general solution to this problem. As proteins generally have smaller partial molar volumes in higher-energy states than in the basic folded state, pressure can shift the equilibrium toward the former substantially, and allows their direct detection and analysis with X-ray crystallography or NMR spectroscopy at elevated pressures. These techniques are now mature, and their status and selected applications are presented with future prospects.
authors.affiliation: Synchrotron Soleil, BP48 Saint Aubin, 91192 Gif sur Yvette, France. roger.fourme@synchrotron-soleil.fr
authors.forename: Roger
authors.initials: R
authors.lastname: Fourme
authors.forename: Eric
authors.initials: E
authors.lastname: Girard
authors.forename: Kazuyuki
authors.initials: K
authors.lastname: Akasaka
mesh_terms: D018360:Crystallography, X-Ray / Q000379:methods*; D046911:Macromolecular Substances / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011312:Pressure
chemical_list: D046911:Macromolecular Substances