ACTH binding to phospholipid bilayers: a 1h-nmr study of the 5-14, 1-14, and 1-24 derivatives

Biopolymers - Nucleic Acid Sciences Section

Volumn 42, Issue 6, 1997, Pages 731-744

  Roux, Michel ^a   Neumann, Jean Michel ^b   Toma, Flavio ^a  

^a CNRS   (France)

^b UNIVERSITÉ DE ROUEN   (France)

Author keywords

ACTH; Lh nmr; Lipid peptide interaction

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; CHEMICAL BONDS; LIPIDS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

PEPTIDES; PHOSPHOLIPIDS;

HORMONES;

CORTICOTROPIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BILAYER MEMBRANE; CARBOXY TERMINAL SEQUENCE; HYDROPHOBICITY; LIGAND BINDING; LIPID VESICLE; MEMBRANE BINDING; MONOLAYER CULTURE; NONHUMAN; PHOSPHOLIPID BILAYER; PROTON NUCLEAR MAGNETIC RESONANCE;

EID: 0031282553     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0282(199711)42:6<731::AID-BIP10>3.0.CO;2-E     Document Type: Article

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