Conformational Flexibility of Bovine Pancreatic Ribonuclease A

スポンサーリンク

概要

• 論文の詳細を見る

• Conformational energies of native ribonuclease A were computed in the multi-dimensional space of dihedral angles of the backbone and side chains. By mini-mization of the total energy starting from three sets of the angles, we obtainedthree low energy conformations, Cl, C2 and C3, which have almost the sameenergy, -644f4kca1/mol and are close to the experimental structure. In theneighborhood of Cl, we found a smooth energy surface with ellipsoidal energycontours. Cl, C2 and C3 were mutttally related with low energy paths in theconformational space. The results indicate that the protein molecule has flexi-bility inside the molecule which arises from the highly cooperative motion of theconstituent atoms. The low energy conformations found in this study account forthe characteristic features experimentally obtained.

• 社団法人日本物理学会の論文
• 1983-12-15

著者

• Ooi Tatsuo

  Institute For Chemical Research Kyoto University

• Ihara Shoji

  Institute For Chemical Research Kyoto University

関連論文

• Determination of Energy Parameters in Lennard-Jones Potentials from Second Virial Coefficients
• Rotational Freedom in Proline Residue
• Tertiary Structure of Proteins. I. : Representation and Computation of the Conformations
• Tertiary Structure of Proteins. II. : Freedom of Dihedral Angles and Energy Calculation
• Energy Surface of Protein Molecule in the Conformational Phase Space
• Molecular Dynamics Study of Ag_3SI
• Conformational Flexibility of Bovine Pancreatic Ribonuclease A
• Thermal stability of a protein predicted from its three dimensional structure
• Molecular dynamics using internal coordinates. I. Infrared spectra of sulfur dioxide.

スポンサーリンク