Comparison of normal mode analysis on a small globular protein in dihedral angle space and Cartesian coordinate space

Kitao, Akio, Hayward, Steven and Go, Nobuhiro (1994) Comparison of normal mode analysis on a small globular protein in dihedral angle space and Cartesian coordinate space. Biophysical Chemistry, 52 (2). pp. 107-114. ISSN 0301-4622

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Abstract

Normal mode analyses on the protein, bovine pancreatic trypsin inhibitor, in dihedral angle space and Cartesian coordinate space are compared. In Cartesian coordinate space it is found that modes of frequencies lower than 30 cm−1 contribute 80% of the total mean-square fluctuation and are represented almost completely by motions in the dihedral angles. Bond angle and length fluctuations dominate in modes above 200 cm−1, but contribute less than 2% to the total mean-square fluctuation. In the low-frequency modes a good correspondence between patterns of atomic displacements was found, but on average the root-mean-square fluctuations of the Cartesian coordinate modes are 13% greater than their dihedral angle counterparts. The main effect of fluctuations in the bond angles and lengths, therefore, is to allow the dihedral angles to become more flexible. As the important subspaces determined from the two methods overlap considerably, dihedral angle space analysis can be applied to proteins too large for Cartesian coordinate space analysis.

Item Type: Article
Faculty \ School: Faculty of Science > School of Computing Sciences
Depositing User: EPrints Services
Date Deposited: 01 Oct 2010 13:41
Last Modified: 29 Apr 2022 01:31
URI: https://ueaeprints.uea.ac.uk/id/eprint/2524
DOI: 10.1016/0301-4622(94)00070-0

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