Structural basis of hierarchical multiple substates of a protein. V: Nonlocal deformations.
Distances between centers of gravity of individual residues are compared among the minimum energy conformations derived from the record of the Monte Carlo simulation of conformational fluctuations in the native state of a globular protein, bovine pancreatic trypsin inhibitor. It is found that local deformations originating from the multiplicity of local conformations cause deformations of the whole structure of the molecule in various ways, which can be classified into two types. Type 1: When a local deformation occurs in a region consisting of a few residues near the surface of the molecule, the whole shape of the molecule responds by deforming elastically. The magnitude of this deformation is in the range of thermal fluctuations calculated by the harmonic approximation around a single minimum. Type 2: We have observed one case belonging to the second type in which local deformations occur cooperatively in an extended region. This region goes across the whole molecule and divide the remaining parts into two. Atom packing changes in and around the extended region of local deformations. For this reason deformation in this region is plastic. Relative location and orientation between the divided two parts change very much. Deformation of the whole shape in this case, associated with the plastic deformation in an extended region, demonstrates that protein molecules have a flexibility beyond the harmonic limit.
Noguti
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Computation Center, Faculty of Engineering, Kyushu University, Fukuoka, Japan.
Go
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D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009010:Monte Carlo Method; D011487:Protein Conformation; D013816:Thermodynamics; D014361:Trypsin Inhibitors
D014361:Trypsin Inhibitors