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400 MHz 1H n.m.r. study of the conformation and self-association of peptidolipin NA
Authors:Marius Ptak  Annie Heitz  Micheline Guinand  Georges Michel
Affiliation:Centre de Biophysique Moléculaire (CNRS) et Université d''Orléans, 1A Avanue de la Recherche Scientifique, 45045 Orléans Cedex, France;Laboratoire de Biochemie Microbienne, Université de Lyon I, 69622 Villeurbanne Cedex, France
Abstract:Peptidolipin NA is a lipocyclopeptide extracted from Nocardia Asteroides having the formula:
/></figure> Its conformation and self-association properties and those of its l-Val(6) analogue have been investigated in three solvents of different polarities: chloroform, pyridine and dimethylsulphoxide, using 400 MHz <sup>1</sup>H n.m.r. A model of the conformation of peptidolipin NA in pyridine has been proposed in which the peptide backbone is folded into a γ-turn around the l-Pro residue. Conformational changes are caused by l-Ala(6) → l-Val(6) replacement and by changing the solvent polarity. Nevertheless, the general shape of the peptide ring seems to be maintained. In chloroform, self-association occurs involving the (2) and, to a lesser extent, the (6) residues. Peptidolipin NA could be representative of natural amphiphiles in which a long hydrophobic tail is bound to a polar peptide moiety.</td> </tr> <tr> <td align=
Keywords:Polypeptide  stereochemistry  lipocyclopeptide  peptidolipin NA  n.m.r.  self association
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