title: Structural basis of hierarchical multiple substates of a protein. III: Side chain and main chain local conformations.
abstract: An analysis is carried out of differences in the minimum energy conformations obtained in the previous paper by energy minimization starting from conformations sampled by a Monte Carlo simulation of conformational fluctuations in the native state of a globular protein, bovine pancreatic trypsin inhibitor. Main conformational differences in each pair of energy minima are found usually localized in several side chains and in a few local main chain segments. Such side chains and local main chain segments are found to take a few distinct local conformations in the minimum energy conformations. Energy minimum conformations can thus be described in terms of combinations of these multiple local conformations.
authors.affiliation: Computation Center, Faculty of Engineering, Kyushu University, Fukuoka, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Noguti
authors.forename: N
authors.initials: N
authors.lastname: Go
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D009010:Monte Carlo Method; D011487:Protein Conformation; D013816:Thermodynamics; D014361:Trypsin Inhibitors
chemical_list: D014361:Trypsin Inhibitors