Comparison of the conformations of cyclolinopeptide A in the solid state and in solution(504 views) Tancredi T, Zanotti G, Rossi F, Benedetti E, Pedone C, Temussi PA
Keywords: Cyclolinopeptide A, Cyclopeptide, Article, Comparative Study, Protein Conformation, Solution And Solubility, Synthesis,
Affiliations: Not available.
References: Not available.
Comparison of the conformations of cyclolinopeptide A in the solid state and in solution
Cyclolinopeptide A, a cyclic nonapeptide isolated from linseed, has lately attracted large interest for its cytoprotective activity. The recent elucidation of its solid state structure has prompted us to undertake a detailed conformational analysis in solution. Room-temperature 1H-nmr spectra in several solvents (DMSO-d6, DMSO-d6/D2O/H2O, CD3OH, (CD3)2CDOH, CDCl3) all show very broad lines, indicating the presence of chemical exchange among several conformers. It proved possible to freeze a single conformational state in CDCl3 at 214 K. Unusual chemical shifts and nuclear Overhauser enhancements are consistent with the main features of the solid state structure.
Comparison of the conformations of cyclolinopeptide A in the solid state and in solution
No results.
Comparison of the conformations of cyclolinopeptide A in the solid state and in solution
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(561 views) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 ViewExport to BibTeXExport to EndNote