Length preferences and periodicity in {beta}-strands. Antiparallel edge {beta}-sheets are more likely to finish in non-hydrogen bonded rings |
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Authors: | Penel, Simon Morrison, R.Gwilym Dobson, Paul D. Mortishire-Smith, Russell J. Doig, Andrew J. |
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Affiliation: | 1Department of Biomolecular Sciences, UMIST, PO Box 88,Manchester M60 1QD and 3Merck, Sharp & Dohme Research Laboratories, Neuroscience Research Centre, Terlings Park, Eastwick Road, Harlow, Essex CM20 2QR, UK 2Present address: Laboratoire de Biometrie et Biologie Evolutive,Bât 711CNRS UMR 5558Université Lyon 1, 43 bd du 11 novembre 1918, 69622 Villeurbanne Cedex, France |
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Abstract: | We analysed the length distributions of different types of ß-strandin a high resolution, non-homologous set of 500 protein structures,finding differences in their mean lengths. Antiparallel edgestrands in strandturnstrand motifs show a preferencefor an even number of residues. This propensity is enhancedif the length is corrected for ß-bulges, which insertan extra residue into the strand. Residues in antiparallel edgeß-strands alternate between being in hydrogen bondedand non-hydrogen bonded rings. Antiparallel edges with an evennumber of residues are more likely to have their final ßresidue in a non-hydrogen bonded ring. This suggests that non-hydrogenbonded rings are intrinsically more stable than hydrogen bondedrings, perhaps because its side chain packing is closer. Therefore,we suggest that a simple way to increase ß-hairpinstability, or the stability of an antiparallel edge strand,is to have a non-hydrogen bonded ring at the end of the strand. Received June 19, 2003; revised October 25, 2003; accepted November 7, 2003 |
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