Tertiary Structure of Proteins. II. : Freedom of Dihedral Angles and Energy Calculation

スポンサーリンク

概要

• 論文の詳細を見る

• By using the procedure described in a preceding paper, several sets of 〓 and ψ are obtained which reproduced similar conformations to the native structure of lysozyme or myoglobin. Contrary to the expectation, the value of f has no maximum along a line connected any two of the minima in the 2n-dimensional phase space. This result shows the existence of many solutions for 〓 and ψ which generate the native conformation under restricted condition of fixed geometry in the main chain. Energy calculation is performed on the conformations obtained above to examine atomic collisions along the main chain. After refinement to remove the collisions, a conformation is finally obtained for lysozyme which has a total energy of -270 kcal/mol and still has an low value of f. Similarly a conformation can be found for myoglobin having an energy of -580 kcal/mol in total.

• 社団法人日本物理学会の論文
• 1972-05-05

著者

• Ooi Tatsuo

  Institute For Chemical Research Kyoto University

• Nishikawa Ken

  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
• 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