Interfacial anchor properties of tryptophan residues in transmembrane peptides can dominate over hydrophobic matching effects in peptide-lipid interactions

Biochemistry

Volumn 42, Issue 18, 2003, Pages 5341-5348

  De Planque, Maurits R R ^a,c   Bonev, Boyan B ^b,f   Demmers, Jeroen A A ^a,c   Greathouse, Denise V ^d   Koeppe II, Roger E ^d   Separovic, Frances ^e   Watts, Anthony ^b   Killian, J Antoinette ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c UTRECHT UNIVERSITY   (Netherlands)

^d UNIVERSITY OF ARKANSAS   (United States)

^e UNIVERSITY OF MELBOURNE   (Australia)

^f UNIVERSITY OF NOTTINGHAM   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DEUTERIUM; HYDROGEN; HYDROPHOBICITY; LIPIDS; NUCLEAR MAGNETIC RESONANCE; SURFACE CHEMISTRY;

HYDROPHOBIC MATCHING;

PROTEINS;

CARBONYL DERIVATIVE; DEUTERIUM; HYDROGEN; INDOLE DERIVATIVE; LIPID; LYSINE; MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; TRYPTOPHAN;

ADAPTATION; ALPHA HELIX; AMINO ACID SEQUENCE; ANALYTIC METHOD; ARTICLE; CORRELATION ANALYSIS; HYDROPHOBICITY; LIPID ANALYSIS; LIPID BILAYER; LIPID MEMBRANE; MASS SPECTROMETRY; MEMBRANE MODEL; NUCLEAR MAGNETIC RESONANCE; PEPTIDE ANALYSIS; POLARIZATION; PRIORITY JOURNAL; PROTEIN LIPID INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE; TECHNIQUE;

ALANINE; CIRCULAR DICHROISM; LEUCINE; LIPID BILAYERS; LYSINE; MAGNETIC RESONANCE SPECTROSCOPY; MEMBRANE PROTEINS; MODELS, CHEMICAL; PEPTIDE FRAGMENTS; PHOSPHATIDYLCHOLINES; PROTEIN STRUCTURE, SECONDARY; TRYPTOPHAN;

EID: 0037881905     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027000r     Document Type: Article

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