期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 469, 期 1, 页码 100-117出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2007.05.015
关键词
energy landscape; protein folding; protein misfolding; aggregation; amyloid fibril formation; intermediate states; oligomers
资金
- Wellcome Trust Funding Source: Medline
Protein aggregation has now become recognised as an important and generic aspect of protein energy landscapes. Since the discovery that numerous human diseases are caused by protein aggregation, the biophysical characterisation of misfolded states and their aggregation mechanisms has received increased attention. Utilising experimental techniques and computational approaches established for the analysis of protein folding reactions has ensured rapid advances in the study of pathways leading to amyloid fibrils and amyloid-related aggregates. Here we describe recent experimental and theoretical advances in the elucidation of the conformational properties of dynamic, heterogeneous and/or insoluble protein ensembles populated on complex, multidimensional protein energy landscapes. We discuss current understanding of aggregation mechanisms in this context and describe how the synergy between biochemical, biophysical and cell-biological experiments are beginning to provide detailed insights into the partitioning of non-native species between protein folding and aggregation pathways. (C) 2007 Elsevier Inc. All rights reserved.
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