Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels-Reference-Cited by-同舟云学术

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Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels

Published:2004-05 Issue:1 Volume:168 Page:153-163
ISSN:1090-7807
Container-title:Journal of Magnetic Resonance
language:en
Short-container-title:Journal of Magnetic Resonance

Author:

Glaser Ralf W.,Sachse Carsten,Dürr Ulrich H.N.,Wadhwani Parvesh,Ulrich Anne S.

Publisher

Elsevier BV

Subject

Condensed Matter Physics,Nuclear and High Energy Physics,Biochemistry,Biophysics

Reference25 articles.

1. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy;Castellani;Nature,2002

2. Membrane protein NMR studies;Opella;Methods Mol. Biol.,2003

3. Solid-state nuclear magnetic resonance investigation of protein and polypeptide structure;Fu;Annu. Rev. Biophys. Biomol. Struct.,1999

4. NMR structural studies of membrane proteins;Marassi;Curr. Opin. Struct. Biol.,1998

5. Membrane-bound structure and alignment of the antimicrobial beta-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMR;Salgado;J. Biomol. NMR,2001

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