Binding of peptides with basic and aromatic residues to bilayer membranes. Phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer

Journal of Biological Chemistry

Volumn 278, Issue 24, 2003, Pages 21459-21466

  Zhang, Wenyi ^a   Crocker, Evan ^a   McLaughlin, Stuart ^a   Smith, Steven O ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; ELECTROSTATICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; POLYPEPTIDES; PRESSURE EFFECTS;

PLASMA MEMBRANES;

PROTEINS;

MARCKS PROTEIN; N METHYL DEXTRO ASPARTIC ACID; NEUROMODULIN; PHENYLALANINE; PHOSPHATE; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHOLIPASE D;

ARTICLE; BILAYER MEMBRANE; CELL MEMBRANE; ELECTRICITY; ENZYME SUBSTRATE; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

ALANINE; CELL MEMBRANE; DIMYRISTOYLPHOSPHATIDYLCHOLINE; ESTERS; LIPID BILAYERS; LIPID METABOLISM; LIPIDS; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; PEPTIDE BIOSYNTHESIS; PEPTIDES; PHENYLALANINE; PHOSPHATIDYLGLYCEROLS; PHOSPHATIDYLINOSITOL 4,5-DIPHOSPHATE; PHOSPHOLIPASE D; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, N-METHYL-D-ASPARTATE; SIGNAL TRANSDUCTION;

EID: 0037821876     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M301652200     Document Type: Article

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