title: Structure and dynamics of the water around myoglobin.
abstract: The interplay between simulations at various levels of hydration and experimental observables has led to a picture of the role of solvent in thermodynamics and dynamics of protein systems. One of the most studied protein-solvent systems is myoglobin, which serves as a paradigm for the development of structure-function relationships in many biophysical studies. We review here some aspects of the solvation of myoglobin and the resulting implications. In particular, recent theoretical and simulation studies unify much of the diverse set of experimental results on water near proteins.
authors.affiliation: W.M. Keck Center for Computational Biology, Houston, Texas 77005-1892, USA.
authors.forename: G N
authors.initials: GN
authors.lastname: Phillips
authors.forename: B M
authors.initials: BM
authors.lastname: Pettitt
mesh_terms: D018360:Crystallography, X-Ray; D004578:Electron Spin Resonance Spectroscopy; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D014867:Water / Q000737:chemistry* / Q000378:metabolism; D014961:X-Ray Diffraction
chemical_list: D009211:Myoglobin; D014867:Water