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Volumn 1545, Issue 1-2, 2001, Pages 153-159
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Solution structure of micelle-bound H5 peptide (427-452): A primary structure corresponding to the pore forming region of the voltage dependent potassium channel
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Author keywords
Ion channel; Micelle; Nuclear magnetic resonance; Three dimensional structure
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Indexed keywords
H5 PEPTIDE;
PEPTIDE;
POTASSIUM CHANNEL;
UNCLASSIFIED DRUG;
ALPHA HELIX;
AMINO ACID SEQUENCE;
ARTICLE;
CHANNEL GATING;
MICELLE;
NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;
PRIORITY JOURNAL;
PROTEIN CONFORMATION;
PROTEIN ISOLATION;
PROTEIN TERTIARY STRUCTURE;
SEQUENCE ANALYSIS;
STREPTOMYCES LIVIDANS;
STRUCTURE ANALYSIS;
AMINO ACID MOTIFS;
AMINO ACID SEQUENCE;
CIRCULAR DICHROISM;
MAGNETIC RESONANCE SPECTROSCOPY;
MICELLES;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
PEPTIDE FRAGMENTS;
POTASSIUM CHANNELS;
PROTEIN STRUCTURE, TERTIARY;
SHAKER SUPERFAMILY OF POTASSIUM CHANNELS;
SOLUTIONS;
STREPTOMYCES LIVIDANS;
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EID: 0035830743
PISSN: 01674838
EISSN: None
Source Type: Journal
DOI: 10.1016/S0167-4838(00)00273-9 Document Type: Article |
Times cited : (4)
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References (17)
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