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The α‐sheet: A missing‐in‐action secondary structure?
Author(s) -
Babin Volodymyr,
Roland Christopher,
Sagui Celeste
Publication year - 2011
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22935
Subject(s) - beta sheet , protein secondary structure , amyloid fibril , metastability , chemistry , conformational isomerism , molecular dynamics , amyloid (mycology) , action (physics) , biophysics , protein structure , biology , physics , computational chemistry , amyloid β , biochemistry , medicine , molecule , organic chemistry , pathology , inorganic chemistry , disease , quantum mechanics
The α‐sheet has been speculated to play a role as a toxic conformer in amyloid diseases. However, except for relatively short fragments, its detection has remained elusive. Here, we present molecular dynamics simulations that support the existence of the α‐sheet as a stable, metastable, or long‐lived secondary structure in polyglutamine and, to a lesser extent, in polyasparagine aggregates. Proteins 2011. © 2010 Wiley‐Liss, Inc.
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