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Volumn 65, Issue 1, 2002, Pages 21-31
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Trifluoroethanol and binding to model membranes stabilize a predicted turn in a peptide corresponding to the first extracellular loop of the angiotensin II AT1A receptor
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Author keywords
CD; Extracellular loop; Fluorescence; G protein coupled receptor; NMR; Peptide membrane interaction; Trifluoroethanol
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Indexed keywords
ANISOTROPY;
CRYSTAL STRUCTURE;
FLUORESCENCE;
HYDROGEN BONDS;
ISOMERS;
MICELLES;
NUCLEAR MAGNETIC RESONANCE;
PHOSPHOLIPIDS;
ELECTROSTATIC INTERACTION;
BIOLOGICAL MEMBRANES;
ANGIOTENSIN 1 RECEPTOR;
PEPTIDE HORMONE;
RHODOPSIN;
TRIFLUOROETHANOL;
AMINO ACID SEQUENCE;
ANISOTROPY;
AQUEOUS SOLUTION;
ARTICLE;
CIRCULAR DICHROISM;
CRYSTAL STRUCTURE;
ELECTRICITY;
FLUORESCENCE ANALYSIS;
HYDROGEN BOND;
IONIZATION;
ISOMER;
MEMBRANE BINDING;
MEMBRANE STABILIZATION;
MOLECULAR INTERACTION;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PROTEIN CONFORMATION;
PROTEIN STABILITY;
PROTON NUCLEAR MAGNETIC RESONANCE;
RECEPTOR BINDING;
SOLUBILITY;
CIRCULAR DICHROISM;
FLUORESCENCE;
HYDROGEN-ION CONCENTRATION;
MAGNETIC RESONANCE SPECTROSCOPY;
MICELLES;
MODELS, BIOLOGICAL;
PROTEIN FOLDING;
RECEPTOR, ANGIOTENSIN, TYPE 1;
RECEPTORS, ANGIOTENSIN;
SODIUM DODECYL SULFATE;
TRIFLUOROETHANOL;
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EID: 0037026868
PISSN: 00063525
EISSN: None
Source Type: Journal
DOI: 10.1002/bip.10209 Document Type: Article |
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Times cited : (15)
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References (60)
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