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Volumn 21, Issue 3, 2001, Pages 191-208

Membrane-bound structure and alignment of the antimicrobial β-sheet peptide gramicidin S derived from angular and distance constraints by solid state 19F-NMR

(6) Salgado, J a Grage, S L a Kondejewski, L H b Hodges, R S b McElhaney, R N b Ulrich, A S a

a FRIEDRICH SCHILLER UNIVERSITY JENA (Germany)

b UNIVERSITY OF ALBERTA (Canada)

Author keywords

4 fluoro phenylglycine; Amphiphilic antimicrobial peptide; Chemical shift anisotropy; CPMG multipulse experiment; Cyclic beta sheet peptide; Distance measurement; Fluorine labelling; Homonuclear dipolar coupling; Macroscopically aligned membrane sample; Segmental orientation

Indexed keywords

CYCLOPEPTIDE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; FLUORINE; GRAMICIDIN S; LEUCINE; MEMBRANE ENZYME; PHENYLGLYCINE;

ANISOTROPY; ANTIMICROBIAL ACTIVITY; ARTICLE; BETA SHEET; CONTROLLED STUDY; LIPID BILAYER; LIPID MEMBRANE; LIQUID CRYSTAL; MEMBRANE STRUCTURE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REPORTER GENE; SOLID STATE; STRUCTURE ACTIVITY RELATION; TEMPERATURE DEPENDENCE;

ANTI-BACTERIAL AGENTS; BACTERIA; CELL MEMBRANE; CIRCULAR DICHROISM; DIMYRISTOYLPHOSPHATIDYLCHOLINE; FLUORINE; GRAMICIDIN; LIPID BILAYERS; MEMBRANE PROTEINS; MICROBIAL SENSITIVITY TESTS; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 0035208239 PISSN: 09252738 EISSN: None Source Type: Journal
DOI: 10.1023/A:1012946026231 Document Type: Article

Times cited : (117)

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