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Volumn 9, Issue 11, 2000, Pages 2118-2127
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Internal motional amplitudes and correlated bond rotations in an α-helical peptide derived from 13C and 15N NMR relaxation
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Author keywords
13C and 15N relaxation; Anisotropic tumbling; Correlated motions; Molecular dynamics; NMR; Peptide; Trifluoroethanol; helix
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Indexed keywords
AMINO ACID DERIVATIVE;
CARBON;
CARBON 13;
GLYCYLPHENYLALANYLSERYLLYSYLALANYLGLUTAMINYLLEUCYLALANYLLYSYLALANYLARGINYLA LANYLALANYLLYSYLARGINYLGLYCYLGLYCYLTYROSINE;
HYDROGEN;
NITROGEN 15;
PEPTIDE;
TRIFLUOROETHANOL;
UNCLASSIFIED DRUG;
WATER;
ALPHA HELIX;
AMPLITUDE MODULATION;
ANISOTROPY;
ARTICLE;
CARBON NUCLEAR MAGNETIC RESONANCE;
MOTION;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN FOLDING;
PROTEIN MOTIF;
PROTEIN STABILITY;
AMINO ACID SEQUENCE;
ANISOTROPY;
CARBON;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, CHEMICAL;
MODELS, STATISTICAL;
MOLECULAR SEQUENCE DATA;
NITROGEN;
PEPTIDES;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, SECONDARY;
PROTONS;
TEMPERATURE;
THERMODYNAMICS;
TRIFLUOROETHANOL;
WATER;
BIKINIA LE-TESTUI;
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EID: 0034486194
PISSN: 09618368
EISSN: None
Source Type: Journal
DOI: 10.1110/ps.9.11.2118 Document Type: Article |
Times cited : (10)
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References (26)
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