Literature DB >> 12505150

Ring and zipper formation is the key to understanding the structural variety in all-beta proteins.

Ryotaro Koike1, Kengo Kinoshita, Akinori Kidera.   

Abstract

A novel structural classification of beta proteins is presented from the viewpoint of the ring-shaped structure and the zipper-like contact pattern, based on the fact that 92% and 60% of beta proteins have the ring topology and the zippered contact pattern, respectively. We discuss the implication of the unexpectedly high preference for the ring and zippered structures in connection with the folding process of beta proteins.

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Year:  2003        PMID: 12505150     DOI: 10.1016/s0014-5793(02)03729-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Phylogeny of protein-folding trajectories reveals a unique pathway to native structure.

Authors:  Motonori Ota; Mitsunori Ikeguchi; Akinori Kidera
Journal:  Proc Natl Acad Sci U S A       Date:  2004-12-10       Impact factor: 11.205

2.  Itinerary profiling to analyze a large number of protein-folding trajectories.

Authors:  Motonori Ota; Mitsunori Ikeguchi; Akinori Kidera
Journal:  Biophys Physicobiol       Date:  2016-11-18

3.  An enhanced partial order curve comparison algorithm and its application to analyzing protein folding trajectories.

Authors:  Hong Sun; Hakan Ferhatosmanoglu; Motonori Ota; Yusu Wang
Journal:  BMC Bioinformatics       Date:  2008-08-18       Impact factor: 3.169

  3 in total

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