4.6 Review

Principles of protein folding, misfolding and aggregation

Journal

SEMINARS IN CELL & DEVELOPMENTAL BIOLOGY
Volume 15, Issue 1, Pages 3-16

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.semcdb.2003.12.008

Keywords

amyloid formation; biological self-assembly; energy landscape; molecular evolution; neurodegenerative disease

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This review summarises our current understanding of the underlying and universal mechanism by which newly synthesised proteins achieve their biologically functional states. Protein molecules, however, all have a finite tendency either to misfold, or to fail to maintain their correctly folded states, under some circumstances. This article describes some of the consequences of such behaviour, particularly in the context of the aggregation events that are frequently associated with aberrant folding. It focuses in particular on the emerging links between protein aggregation and the increasingly prevalent forms of debilitating disease with which it is now known to be associated. (C) 2003 Elsevier Ltd. All rights reserved.

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