PS - a program for the analysis of helix geometry
- Author(s)
- Smith, BJ;
- Journal Title
- JOURNAL OF MOLECULAR GRAPHICS & MODELLING
- Publication Type
- Journal Article
- Abstract
- The structure of helices within proteins is often distorted from the ideal linear topology. Curvature of the helix axis can be measured by determining the radius of a circle fit to the axis. Described here is a method of defining a curved path that places backbone atoms (usually C alpha) equidistantly from the path. The variance in the distance of backbone atoms from the helix axis is minimised to produce the parametric equations that describe the intersection of a sphere and a plane. The geometric properties of the helix (including helix radius, radius of curvature, and pitch) can be readily obtained from these equations. The approach is applicable to any form of helix, can use any atom in the peptide to determine the axis, can be applied to any polypeptide including mixed alpha/beta peptides, and does not rely on a regular spacing of peptide monomers in the polypeptide chain. (C) 2011 Elsevier Inc. All rights reserved.
- Publisher
- ELSEVIER SCIENCE INC
- Keywords
- CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; COILED COILS; ATOMIC-RESOLUTION; 1.4-A RESOLUTION; ALPHA-HELICES; PROTEIN; ACID; POLYPEPTIDE; REFINEMENT
- Research Division(s)
- Structural Biology
- Publisher's Version
- https://doi.org/10.1016/j.jmgm.2011.11.004
- Terms of Use/Rights Notice
- Copyright © 2011 Elsevier Inc. All rights reserved.
Creation Date: 2012-03-01 12:00:00