Position and ionization state of Asp in the core of membrane-inserted α helices control both the equilibrium between transmembrane and nontransmembrane helix topography and transmembrane helix positioning

Biochemistry

Volumn 43, Issue 27, 2004, Pages 8794-8806

  Caputo, Gregory A ^a,b   London, Erwin ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b TEXAS A M COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FLUORESCENCE; HYDROPHOBICITY; IONIZATION; PH EFFECTS; POLYPEPTIDES; QUENCHING;

BILAYER SURFACES; HELICAL STATES; IONIZATION STATES;

BIOCHEMISTRY;

AMINO ACID; ASPARTIC ACID; DIOLEOYLPHOSPHATIDYLCHOLINE; LEUCINE; LYSINE; POLYPEPTIDE; SYNTHETIC PEPTIDE;

ARTICLE; BILAYER MEMBRANE; CIRCULAR DICHROISM; ENDOSOME; FLUORESCENCE; HYDROPHOBICITY; IONIZATION; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MEMBRANE MODEL; MEMBRANE VESICLE; PEPTIDE SYNTHESIS; PH; PRIORITY JOURNAL; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SPECTROFLUOROMETRY;

ASPARTIC ACID; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; IONS; LIPOSOMES; MEMBRANE LIPIDS; MEMBRANE PROTEINS; PEPTIDES; PHOSPHATIDYLCHOLINES; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; TRYPTOPHAN;

EID: 3042774119     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049696p     Document Type: Article

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