Threshold hydrophobicity dictates helical conformations of peptides in membrane environments

Biopolymers

Volumn 39, Issue 3, 1996, Pages 465-470

  Liu, Li Ping ^b   Li, Shun Cheng ^a   Goto, Natalie K ^b   Deber, Charles M ^b  

^a MOUNT SINAI HOSPITAL   (Canada)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; COMPOSITION; CONFORMATIONS; MEMBRANES; SPECTROSCOPY;

COMPOSITIONAL ANALYSES; FLUORESCENCE SPECTROSCOPY; MEMBRANE MIMETIC MEDIA; PEPTIDES; THRESHOLD HYDROPHOBICITY; TRANSMEMBRANE SEGMENTS;

PROTEINS;

MEMBRANE PROTEIN; SYNTHETIC PEPTIDE;

AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE SPECTROSCOPY; HYDROPHOBICITY; MEMBRANE MODEL; MEMBRANE VESICLE; MICELLE; PEPTIDE ANALYSIS; PEPTIDE SYNTHESIS;

AMINO ACID SEQUENCE; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MICELLES; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

EID: 0030249150     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(sici)1097-0282(199609)39:3<465::aid-bip17>3.0.co;2-a     Document Type: Article

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