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Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers.

Abstract:

The interaction with model membranes of a peptide, EqtII(1-32), corresponding to the N-terminal region of the pore-forming toxin equinatoxin II (EqtII) has been studied using solid-state NMR and molecular dynamics (MD) simulations. The distances between specifically labeled nuclei in [(19)F-para]Phe16-[1-(13)C]Leu19 and [(19)F-para]Phe16-[(15)N]Leu23 analogs of EqtII(1-32) measured by REDOR in lyophilized peptide were in agreement with published crystal and solution structures. However, in bo...

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Publication status:
Published

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Publisher copy:
10.1002/prot.22612

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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Role:
Author
Journal:
Proteins
Volume:
78
Issue:
4
Pages:
858-872
Publication date:
2010-03-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:e6184bfd-f36b-4108-a6fb-e8b92ad28d71
Source identifiers:
99774
Local pid:
pubs:99774

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