✦ LIBER ✦

Peptide secondary structure induced by a micellar phospholipidic interface: proton NMR conformational study of a lipopeptide

✍ Scribed by Macquaire, Francois; Baleux, Francoise; Giaccobi, Emmanuelle; Huynh Dinh Tam, ; Neumann, Jean Michel; Sanson, Alain

Book ID: 117997728
Publisher: American Chemical Society
Year: 1992
Tongue: English
Weight: 796 KB
Volume: 31
Category: Article
ISSN: 0006-2960
DOI: 10.1021/bi00124a018

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Two- and three-dimensional proton NMR st

Two- and three-dimensional proton NMR studies of a wheat phospholipid transfer protein: sequential resonance assignments and secondary structure

✍ Simorre, Jean Pierre; Caille, Anita; Marion, Dominique; Marion, Didier; Ptak, Ma 📂 Article 📅 1991 🏛 American Chemical Society 🌐 English ⚖ 976 KB

Conformation of colipase: Prediction of

Conformation of colipase: Prediction of the secondary structure, circular dichroism and 360 MHz proton NMR studies of porcine colipase A

✍ Paul Canioni; Patrick J. Cozzone; Louis Sarda 📂 Article 📅 1980 🏛 Elsevier Science ⚖ 991 KB

Conformational changes in phospholipase

Conformational changes in phospholipase A2 upon binding to micellar interfaces in the absence and presence of competitive inhibitors. A proton and nitrogen-15 NMR study

✍ Peters, Anton R.; Dekker, Niek; Van den Berg, Lambertus; Boelens, Rolf; Kaptein, 📂 Article 📅 1992 🏛 American Chemical Society 🌐 English ⚖ 750 KB

Conformational study of bacterial lipope

Conformational study of bacterial lipopeptides: Refinement of the structure of iturin A in solution by two-dimensional 1H-nmr and energy calculations

✍ Dominique Marion; Monique Genest; Anita Caille; Françoise Peypoux; Georges Miche 📂 Article 📅 1986 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 958 KB

Iturin A is a lipopeptide extracted from strains of Bacillus snbtilis. Seven peptide residues form a cycle closed by a &amino acid carrying a hydrophobic tail. This compound is an antifungal and induces the formation of conducting pores in black lipid membranes. Two-dimensional 'H-nmr was used for i

The secondary structure of human plasma

The secondary structure of human plasma fibronectin: conformational changes induced by acidic pH and elevated temperatures; a circular dichroic study

✍ Eija Österlund 📂 Article 📅 1988 🏛 Elsevier Science 🌐 English ⚖ 635 KB

Conformational study of a collagen pepti

Conformational study of a collagen peptide by 1H NMR spectroscopy: observation of the 14N-1H spin-spin coupling of the Arg guanidinium moiety in the triple-helix structure

✍ Roberto Consonni; Laura Santomo; Ruggero Tenni; Renato Longhi; Lucia Zetta 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 112 KB