Efficient characterization of protein secondary structure in terms of screw motions

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 crystallography and by structural NMR measurements are used.
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https://hal.archives-ouvertes.fr/hal-00088869
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Submitted on : Monday, August 7, 2006 - 2:32:06 PM
Last modification on : Friday, June 14, 2019 - 3:12:13 PM

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G.R. Kneller, P. Calligari. Efficient characterization of protein secondary structure in terms of screw motions. Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2006, 62, pp.302-311. ⟨10.1107/S0907444905042654⟩. ⟨hal-00088869⟩

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