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A Two-Tailed Phosphopeptide Crystallizes to Form a Lamellar Structure

Abstract:

The crystal structure of a designed phospholipid-inspired amphiphilic phosphopeptide at 0.8 Å resolution is presented. The phosphorylated β-hairpin peptide crystallizes to form a lamellar structure that is stabilized by intra- and intermolecular hydrogen bonding, including an extended β-sheet structure, as well as aromatic interactions. This first reported crystal structure of a two-tailed peptidic bilayer reveals similarities in thickness to a typical phospholipid bilayer. However, water mol...

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

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Publisher copy:
10.1002/anie.201609877

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Institution:
University of Oxford
Department:
Merton College
Role:
Author
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Grant:
Horizon 2020 BI-SON-694426
Publisher:
Wiley-VCH Publisher's website
Journal:
Angewandte Chemie International Edition Journal website
Volume:
56
Issue:
12
Pages:
3252-3255
Publication date:
2017-02-13
Acceptance date:
2017-01-18
DOI:
EISSN:
1521-3773
ISSN:
1433-7851
Pubs id:
pubs:681972
URN:
uri:a12c8810-5dee-4ba8-9baa-7c0e8462e0bc
UUID:
uuid:a12c8810-5dee-4ba8-9baa-7c0e8462e0bc
Local pid:
pubs:681972
Paper number:
12

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