- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1002/prot.22612
-
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- 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
- Copyright date:
- 2010
Journal article
Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers.
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