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Article Dans Une Revue Journal of Theoretical Biology Année : 2010

Conformational characterization of disulfide bonds: A tool for protein classification

Rute R. da Fonseca
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Brett Drury
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Résumé

Throughout evolution, mutations in particular regions of some protein structures have resulted in extra covalent bonds that increase the overall robustness of the fold: disulfide bonds. The two strategically placed cysteines can also have a more direct role in protein function, either by assisting thiol or disulfide exchange, or through allosteric effects. In this work, we verified how the structural similarities between disulfides can reflect functional and evolutionary relationships between different proteins. We analyzed the conformational patterns of the disulfide bonds in a set of disulfide-rich proteins that included twelve superfamilies: thioredoxin-like and eleven superfamilies containing small disulfide-rich proteins ().
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Dates et versions

hal-00634004 , version 1 (20-10-2011)

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José Rui Ferreira Marques, Rute R. da Fonseca, Brett Drury, André Melo. Conformational characterization of disulfide bonds: A tool for protein classification. Journal of Theoretical Biology, 2010, 267 (3), pp.388. ⟨10.1016/j.jtbi.2010.09.012⟩. ⟨hal-00634004⟩

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