Open AccessDTA: dihedral transition analysis for characterization of the effects of large main-chain dihedral changes in proteins
Author(s) -
Wataru Nishima,
Guoying Qi,
Steven Hayward,
Akio Kitao
Publication year - 2009
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/btp032
Subject(s) - dihedral angle , chemistry , crystallography , molecule , organic chemistry , hydrogen bond
The biological function of proteins is associated with a variety of motions, ranging from global domain motion to local motion of side chain. We propose a method, dihedral transition analysis (DTA), to identify significant dihedral angle changes between two distinct protein conformations and for characterization of the effect of these transitions on both local and global conformation.
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