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Volumn 1511, Issue 1, 2001, Pages 60-73
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Differential scanning calorimetry and 2H nuclear magnetic resonance and Fourier transform infrared spectroscopy studies of the effects of transmembrane α-helical peptides on the organization of phosphatidylcholine bilayers
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Author keywords
IR spectroscopy; Lipid; Lipid chain order; NMR spectroscopy; Transmembrane peptide
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Indexed keywords
MEMBRANE PROTEIN;
PHOSPHATIDYLCHOLINE;
ALPHA HELIX;
ARTICLE;
CIRCULAR DICHROISM;
CONFORMATION;
CRYSTAL STRUCTURE;
DEUTERON NUCLEAR MAGNETIC RESONANCE;
DIFFERENTIAL SCANNING CALORIMETRY;
ELECTRON SPIN RESONANCE;
ENTHALPY;
INFRARED SPECTROSCOPY;
LIPID BILAYER;
LIPOPHILICITY;
PRIORITY JOURNAL;
CALORIMETRY, DIFFERENTIAL SCANNING;
LIPID BILAYERS;
MAGNETIC RESONANCE SPECTROSCOPY;
MEMBRANE LIPIDS;
MEMBRANE PROTEINS;
MOLECULAR CONFORMATION;
PEPTIDES;
PHOSPHATIDYLCHOLINES;
SPECTROSCOPY, FOURIER TRANSFORM INFRARED;
SURFACE PROPERTIES;
TEMPERATURE;
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EID: 0035831154
PISSN: 00052736
EISSN: None
Source Type: Journal
DOI: 10.1016/S0005-2736(00)00382-5 Document Type: Article |
Times cited : (40)
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References (44)
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