NDLI: Structure of the 21–30 fragment of amyloid β-protein

Content Provider	PubMed Central
Author	Baumketner, Andrij Bernstein, Summer L. Wyttenbach, Thomas Lazo, Noel D. Teplow, David B. Bowers, Michael T. Shea, Joan-emma
Abstract	Folding and self-assembly of the 42-residue amyloid β-protein (Aβ) are linked to Alzheimer's disease (AD). The 21–30 region of Aβ, Aβ(21–30), is resistant to proteolysis and is believed to nucleate the folding of full-length Aβ. The conformational space accessible to the Aβ(21–30) peptide is investigated by using replica exchange molecular dynamics simulations in explicit solvent. Conformations belonging to the global free energy minimum (the “native” state) from simulation are in good agreement with reported NMR structures. These conformations possess a bend motif spanning the central residues V24–K28. This bend is stabilized by a network of hydrogen bonds involving the side chain of residue D23 and the amide hydrogens of adjacent residues G25, S26, N27, and K28, as well as by a salt bridge formed between side chains of K28 and E22. The non-native states of this peptide are compact and retain a native-like bend topology. The persistence of structure in the denatured state may account for the resistance of this peptide to protease degradation and aggregation, even at elevated temperatures.
Related Links	http://dx.doi.org/10.1110/ps.062076806
Ending Page	1247
Page Count	9
Starting Page	1239
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	6
Volume Number	15
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2006-06-01
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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