Folding of small disulfide-rich proteins : clarifying the puzzle
Arolas, Joan L. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Ventura, Salvador (Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Avilés, Francesc X. (Francesc Xavier)
(Universitat Autònoma de Barcelona. Departament de Bioquímica i de Biologia Molecular)
Chang, Jui-Yoa (The University of Texas. Institute of Molecular Medicine)
Date: |
2006 |
Abstract: |
The process by which small proteins fold to their native conformations has been intensively studied over the last few decades. In this field, the particular chemistry of disulfide bond formation has facilitated the characterization of the oxidative folding of numerous small, disulfide-rich proteins with results that illustrate a high diversity of folding mechanisms, differing in the heterogeneity and disulfide pairing nativeness of their intermediates. In this review, we combine information on the folding of different protein models together with the recent structural determinations of major intermediates to provide new molecular clues in oxidative folding. Also, we turn to analyze the role of disulfide bonds in misfolding and protein aggregation and their implications in amyloidosis and conformational diseases. |
Note: |
Premi a l'excel·lència investigadora. Àmbit de les Ciències Experimentals. 2008 |
Rights: |
Tots els drets reservats. |
Language: |
Anglès |
Document: |
Article ; recerca ; Versió acceptada per publicar |
Subject: |
PREI 2008 |
Published in: |
Trends in Biochemical Sciences, Vol. 31, Núm. 5 (2006) , p. 292-301, ISSN 1362-4326 |
DOI: 10.1016/j.tibs.2006.03.005
Post-print
31 p, 611.6 KB
|
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Record created 2011-02-21, last modified 2022-09-06