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Solid-State NMR Analysis of the PGLa Peptide Orientation in DMPC Bilayers: Structural Fidelity of (2)H-Labels versus High Sensitivity of (19)F-NMR

The structure and alignment of the amphipathic α-helical antimicrobial peptide PGLa in a lipid membrane is determined with high accuracy by solid-state (2)H-NMR. Orientational constraints are derived from a series of eight alanine-3,3,3-d(3)-labeled peptides, in which either a native alanine is nonp...

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Hlavní autoři: Strandberg, Erik, Wadhwani, Parvesh, Tremouilhac, Pierre, Dürr, Ulrich H. N., Ulrich, Anne S.
Médium: Artigo
Jazyk:Inglês
Vydáno: Biophysical Society 2006
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1367318/
https://ncbi.nlm.nih.gov/pubmed/16339890
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1529/biophysj.105.073858
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