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Structure-activity relationship of amyloid fibrils

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Title Structure-activity relationship of amyloid fibrils
 
Creator MAJI, SK
WANG, L
GREENWALD, J
RIEK, R
 
Subject amyloid
fibril
protein
aggregation
nuclear magnetic resonance
alzheimer's disease
solid-state nmr
nuclear-magnetic-resonance
beta-sheet structure
probing solvent accessibility
alpha-synuclein fibrils
prion protein-fragment
ray fiber diffraction
het-s prion
secondary structure
molecular-conformation
 
Description Protein aggregation is a process in which proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as either amorphous or highly ordered, the most common form of the latter being amyloid fibrils. Amyloid fibrils composed of cross-beta-sheet structure are the pathological hallmarks of several diseases including Alzheimer's disease, but are also associated with functional states such as the fungal HET-s prion. This review aims to summarize the recent high-resolution structural studies of amyloid fibrils in light of their ( potential) activities. We propose that the repetitive nature of the cross-beta-sheet structure of amyloids is key for their multiple properties: the repeating motifs can translate a rather non-specific interaction into a specific one through cooperativity. (C) 2009 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
 
Publisher ELSEVIER SCIENCE BV
 
Date 2011-10-12T11:32:17Z
2011-12-15T09:16:05Z
2011-10-12T11:32:17Z
2011-12-15T09:16:05Z
2009
 
Type Review
 
Identifier FEBS LETTERS,583(16)2610-2617
0014-5793
http://dx.doi.org/10.1016/j.febslet.2009.07.003
http://dspace.library.iitb.ac.in/xmlui/handle/10054/13758
http://hdl.handle.net/100/2992
 
Language en