Title

Determination of helix orientations in proteins

Authors

Authors

S. A. Tatulian

Comments

Authors: contact us about adding a copy of your work at STARS@ucf.edu

Abbreviated Journal Title

Comput. Biol. Chem.

Keywords

Protein structure; Helix orientation; Computational analysis; MEMBRANE-PROTEINS; PACKING; AXIS; PREFERENCES; CALMODULIN; PROGRAM; MOTIFS; ANGLE; Biology; Computer Science, Interdisciplinary Applications

Abstract

Accurate description of helices, including Curvature and bending, and determination of interhelical angles are essential for analysis of the three-dimensional fold and functionally important conformational changes in helical proteins. Here, a new computational method is presented that allows determination of angles between any helical stretches,the radius of curvature of curved helices, bending angle of bent helices, as well as symmetry relations within the protein molecule, using main chain atom coordinates. The method has been applied to describe changes in interhelical angles in calmodulin upon interaction with a target peptide, which reveals the conformational changes at a higher precision. Because subtle changes in helix-to-helix packing and interhelical angles often underlie significant functional transitions in proteins, this approach can serve as a useful tool for Characterization of such conformational changes at an exceedingly high accuracy and thus provide detailed insight into the structure-function relationship of proteins. (c) 2008 Elsevier Ltd. All rights reserved.

Journal Title

Computational Biology and Chemistry

Volume

32

Issue/Number

5

Publication Date

1-1-2008

Document Type

Article

Language

English

First Page

370

Last Page

374

WOS Identifier

WOS:000260110700009

ISSN

1476-9271

Share

COinS