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Conformational preferences of a 14-residue fibrillogenic peptide from acetylcholinesterase

Abstract:

A 14-residue fragment from near the C-terminus of the enzyme acetylcholinesterase (AChE) is believed to have a neurotoxic/neurotrophic effect acting via an unknown pathway. While the peptide is α-helical in the full-length enzyme, the structure and association mechanism of the fragment are unknown. Using multiple molecular dynamics simulations, starting from a tetrameric complex of the association domain of AChE and systematicall disassembled subsets that include the peptide fragment, we show...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1021/bi1001807

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Institution:
University of Oxford
Department:
Medical Sciences Division - Biochemistry
Role:
Author
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Institution:
University of Oxford
Department:
Medical Sciences Division - Biochemistry
Role:
Author
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Funding agency for:
Philip C. Biggin
Wellcome Trust More from this funder
Publisher:
American Chemical Society Publisher's website
Journal:
Biochemistry Journal website
Volume:
49
Issue:
17
Pages:
3678–3684
Publication date:
2010-01-01
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:81ae01db-27b1-47ef-aab7-71db34e4471d
Local pid:
ora:5974
Language:
English
Subjects:

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