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High torsional energy disulfides : relationship between cross-strand disulfides and right-handed staples

journal contribution
posted on 2006-01-01, 00:00 authored by N Haworth, L Feng, Merridee Wouters
Redox-active disulfides are capable of being oxidized and reduced under physiological conditions. The enzymatic role of redox-active disulfides in thiol-disulfide reductases is well-known, but redox-active disulfides are also present in non-enzymatic protein structures where they may act as switches of protein function. Here, we examine disulfides linking adjacent β-strands (cross-strand disulfides), which have been reported to be redox-active. Our previous work has established that these cross-strand disulfides have high torsional energies, a quantity likely to be related to the ease with which the disulfide is reduced. We examine the relationship between conformations of disulfides and their location in protein secondary structures. By identifying the overlap between cross-strand disulfides and various conformations, we wish to address whether the high torsional energy of a cross-strand disulfide is sufficient to confer redox activity or whether other factors, such as the presence of the cross-strand disulfide in a strained β-sheet, are required.

History

Journal

Journal of bioinformatics and computational biology

Volume

4

Issue

1

Pagination

155 - 168

Publisher

Imperial College Press

Location

London, England

ISSN

1757-6334

eISSN

0219-7200

Language

eng

Publication classification

C1.1 Refereed article in a scholarly journal

Copyright notice

2006, Imperial College Press

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