title: The use of NMR chemical shifts to analyse the MD trajectories: simulation of bovine pancreatic trypsin inhibitor dynamics in water as a test case for solvent influences.
abstract: In this paper the NMR secondary chemical shifts, that are estimated from a set of 3D-structures, are compared with the observed ones to appraise the behaviour of a known x-ray diffraction structure (of the bovine pancreatic trypsin inhibitor protein) when various molecular dynamics are applied. The results of a 200 ps molecular dynamics under various conditions are analysed and different ways to modify the molecular dynamics are considered. With the purpose of avoiding the time-consuming explicit representation of the solvent (water) molecules, an attempt was made to understand the role of the solvent and to develop an implicit representation, which may be refined. A simulation of hydrophobic effects in an aqueous environment is also proposed which seems to provide a better approximation of the observed solution structure of the protein.
authors.affiliation: Unité de Biophysique Structurale, UMR 5471 CNRS, Université Bordeaux 1, 33405 Talence, France.
authors.forename: Bernard
authors.initials: B
authors.lastname: Busetta
authors.forename: Philippe
authors.initials: P
authors.lastname: Picard
authors.forename: Gilles
authors.initials: G
authors.lastname: Precigoux
mesh_terms: D000818:Animals; D007611:Aprotinin / Q000737:chemistry*; D002417:Cattle; D003198:Computer Simulation; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011487:Protein Conformation; D015203:Reproducibility of Results; D012680:Sensitivity and Specificity; D012997:Solvents / Q000737:chemistry*; D055672:Static Electricity; D014867:Water / Q000737:chemistry*
chemical_list: D012997:Solvents; D014867:Water; D007611:Aprotinin