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Volumn 504, Issue 3, 2001, Pages 161-165
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Solid-state NMR investigations of interaction contributions that determine the alignment of helical polypeptides in biological membranes
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Author keywords
Amphipathic peptide; Hydrophobicity scale; Interface; Membrane equilibrium; Oriented bilayer; Transmembrane polypeptide
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Indexed keywords
ALANINE DERIVATIVE;
ANTIBIOTIC AGENT;
HISTIDINE DERIVATIVE;
LEUCINE;
LYSINE DERIVATIVE;
PEPTIDE DERIVATIVE;
PHOSPHOLIPID DERIVATIVE;
VPU PROTEIN;
AMINO TERMINAL SEQUENCE;
CONFERENCE PAPER;
HUMAN IMMUNODEFICIENCY VIRUS 1;
HYDROPHOBICITY;
LIPID MEMBRANE;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PH;
PHOSPHOLIPID BILAYER;
PRIORITY JOURNAL;
PROTEIN INTERACTION;
SOLID STATE;
AMINO ACID SEQUENCE;
CELL MEMBRANE;
HYDROGEN-ION CONCENTRATION;
KINETICS;
LIPID BILAYERS;
MAGNETIC RESONANCE SPECTROSCOPY;
MODELS, BIOLOGICAL;
MOLECULAR SEQUENCE DATA;
PEPTIDES;
PROTEIN CONFORMATION;
PROTEIN STRUCTURE, SECONDARY;
THERMODYNAMICS;
VIRAL PROTEINS;
HUMAN IMMUNODEFICIENCY VIRUS 1;
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EID: 0035979758
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(01)02741-7 Document Type: Conference Paper |
Times cited : (24)
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References (47)
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