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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 alpha-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 systematically disassembled subsets that include the peptide fragment, we...

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Publication status:
Published

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Publisher copy:
10.1021/bi1001807

Authors


Vijayan, R More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Biochemistry
Volume:
49
Issue:
17
Pages:
3678-3684
Publication date:
2010-05-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:d6ff3f39-2b33-4bcb-ba97-6c05134075cf
Source identifiers:
99953
Local pid:
pubs:99953

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