Juxtaposed half-cystines as disulphide bridged partners in protein tertiary structure

dc.contributor.author Guruprasad, Kunchur
dc.contributor.author Kartik, V. Jai
dc.contributor.author Lavanya, T.
dc.contributor.author Guruprasad, Lalitha
dc.date.accessioned 2022-03-27T08:34:02Z
dc.date.available 2022-03-27T08:34:02Z
dc.date.issued 2006-01-01
dc.description.abstract Disulphide bridges involving juxtaposed half-cystines are observed in a number of protein three-dimensional structures analyzed from the Protein Data Bank. These disulphide bridges comprise a 'ring of 8-atoms' corresponding to Cα1-C′-N-Cα2-Cβ2-S γ2-Sγ1-Cβ1-C β1 in the two half-cystines. The presence of such disulphide bridges introduces a 'bend' or 'kink' in the protein polypeptide chain. © 2006 Bentham Science Publishers Ltd.
dc.identifier.citation Protein and Peptide Letters. v.13(6)
dc.identifier.issn 09298665
dc.identifier.uri 10.2174/092986606777145841
dc.identifier.uri http://www.eurekaselect.com/openurl/content.php?genre=article & issn=0929-8665 & volume=13 & issue=6 & spage=577
dc.identifier.uri https://dspace.uohyd.ac.in/handle/1/10856
dc.title Juxtaposed half-cystines as disulphide bridged partners in protein tertiary structure
dc.type Journal. Article
dspace.entity.type
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