In a stable condition: Disulfide bonds stabilize folded proteins primarily by decreasing the entropic cost of folding. Such cross-links also reduce toxic aggregation by favoring the formation of highly structured amyloid fibrils (see picture). It is suggested that disulfide bonds in extracellular proteins were selected by evolutionary pressures because they decrease the propensity to form toxic aggregates. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein / Mossuto, M. F.; Bolognesi, B.; Guixer, B.; Dhulesia, A.; Agostini, F.; Kumita, J. R.; Tartaglia, G. G.; Dumoulin, M.; Dobson, C. M.; Salvatella, X.. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - 50:31(2011), pp. 7048-7051. [10.1002/anie.201100986]
Disulfide bonds reduce the toxicity of the amyloid fibrils formed by an extracellular protein
Tartaglia G. G.;
2011
Abstract
In a stable condition: Disulfide bonds stabilize folded proteins primarily by decreasing the entropic cost of folding. Such cross-links also reduce toxic aggregation by favoring the formation of highly structured amyloid fibrils (see picture). It is suggested that disulfide bonds in extracellular proteins were selected by evolutionary pressures because they decrease the propensity to form toxic aggregates. Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.| File | Dimensione | Formato | |
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