Studies of the minimum hydrophobicity of α-helical peptides required to maintain a stable transmembrane association with phospholipid bilayer membranes

Biochemistry

Volumn 46, Issue 4, 2007, Pages 1042-1054

  Lewis, R N A H ^a   Liu, F ^a   Krivanek, R ^b   Rybar, P ^b   Hianik, T ^b   Flach, C R ^c   Mendelsohn, R ^c   Chen, Y ^d   Mant, C T ^d   Hodges, R S ^d   McElhaney, R N ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

^b Physics and Informatics   (Slovakia)

^c RUTGERS UNIVERSITY   (United States)

^d UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AQUEOUS PHASE; LIPID BILAYER MEMBRANES; SELF-AGGREGATION; TRANSMEMBRANE PEPTIDES;

AMINO ACIDS; FREE ENERGY; HYDROPHOBICITY; LIPIDS; PHOSPHOLIPIDS; PROTEINS;

CELL MEMBRANES;

ACETYLLYSYLGLYCYLLEUCYLLYSYLALANINAMIDE DERIVATIVE; ALANINE; LEUCINE; PHOSPHATIDYLCHOLINE; PHOSPHOLIPID; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; BILAYER MEMBRANE; HYDROPHOBICITY; MEMBRANE MODEL; MOLECULAR STABILITY; NONHUMAN; PEPTIDE ANALYSIS; PHOSPHOLIPID BILAYER; PRIORITY JOURNAL; PROTEIN INTERACTION; REVERSED PHASE HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; SURFACE PROPERTY;

AMINO ACID SEQUENCE; CALORIMETRY, DIFFERENTIAL SCANNING; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CIRCULAR DICHROISM; HYDROPHOBICITY; LIPID BILAYERS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; PEPTIDES; PHOSPHOLIPIDS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

EID: 33846621039     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061891b     Document Type: Article

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