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ScrewFit : combining localization and description of protein secondary structure
Abstract
A simple and efficient method is presented to describe the secondary structure of proteins in terms of orientational distances between consecutive peptide planes and local helix parameters. The method uses quaternion-based superposition fits of the protein peptide planes in conjunction with Chasles’ theorem, which states that any rigid-body displacement can be described by a screw motion. The helix parameters are derived from the best superposition of consecutive peptide planes and the ‘worst’ fit is used to define the orientational distance. Applications are shown for standard secondary-structure motifs of peptide chains for several proteins belonging to different fold classes and for a description of structural changes in lysozyme under hydrostatic pressure. In the latter case, published reference data obtained by X-ray crystallo- graphy and by structural NMR measurements are used.
Kneller, G., and P. Calligari, "ScrewFit : combining localization and description of protein secondary structure", Acta Crystallographica Section D, D62, 302–311.
Authors: Kneller
Calligari
Coders: Calligari
Last update
Wed Jul 29 04:09:00 CEST 2015
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