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Volumn 41, Issue 26, 2002, Pages 8396-8404
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The effects of hydrophobic mismatch between phosphatidylcholine bilayers and transmembrane α-helical peptides depend on the nature of interfacially exposed aromatic and charged residues
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Author keywords
[No Author keywords available]
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Indexed keywords
RESIDUES;
LIPIDS;
PH;
PROTEINS;
BIOCHEMISTRY;
ARGININE;
AROMATIC COMPOUND;
HISTIDINE;
LYSINE;
PHENYLALANINE;
PHOSPHATIDYLCHOLINE;
TRYPTOPHAN;
TYROSINE;
ALPHA HELIX;
ARTICLE;
BINDING AFFINITY;
HYDROPHOBICITY;
LIPID BILAYER;
MISMATCH NEGATIVITY;
PH;
PRIORITY JOURNAL;
PROTEIN LIPID INTERACTION;
THICKNESS;
AMINO ACID SEQUENCE;
CIRCULAR DICHROISM;
LIPID BILAYERS;
MAGNETIC RESONANCE SPECTROSCOPY;
MOLECULAR SEQUENCE DATA;
PEPTIDES;
PHOSPHATIDYLCHOLINES;
PROTEIN STRUCTURE, SECONDARY;
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EID: 0037008040
PISSN: 00062960
EISSN: None
Source Type: Journal
DOI: 10.1021/bi0257686 Document Type: Article |
Times cited : (89)
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References (43)
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