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Titolo:
A strategy for probing the autonomy of cross-domain stereochemical communication in glycoconjugates
Autore:
Live, DH; Wang, ZG; Iserloh, U; Danishefsky, SJ;
Indirizzi:
Mem Sloan Kettering Canc Ctr, Bioorgan Chem Lab, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA Univ Minnesota, Dept Biochem Mol Biol & Biophys, Minneapolis, MN 55455 USAUniv Minnesota Minneapolis MN USA 55455 iophys, Minneapolis, MN 55455 USA
Titolo Testata:
ORGANIC LETTERS
fascicolo: 6, volume: 3, anno: 2001,
pagine: 851 - 854
SICI:
1523-7060(20010322)3:6<851:ASFPTA>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN CHORIONIC-GONADOTROPIN; ADHESION MOLECULE CD2; N-LINKED GLYCAN; CRYSTAL-STRUCTURE; GLYCOSYLATION; GLYCOPEPTIDE; RESOLUTION; PROTEIN; CONFORMATION; CONVERGENT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
26
Recensione:
Indirizzi per estratti:
Indirizzo: Danishefsky, SJ Mem Sloan Kettering Canc Ctr, Bioorgan Chem Lab, 1275 YorkAve, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr 1275 York Ave NewYork NY USA 10021
Citazione:
D.H. Live et al., "A strategy for probing the autonomy of cross-domain stereochemical communication in glycoconjugates", ORG LETT, 3(6), 2001, pp. 851-854

Abstract

[GRAPHICS]Glycoproteins contain carbohydrate and peptide sectors. As a model for studying whether there exists stereochemical "communication" between the two domains, we prepared two glycopeptides differing only in the absolute stereochemistry of the peptide domain (L-peptide vs D-peptide), High-field NMR spectroscopy revealed that there are distinct and measurable differences, indicating that the two domains are at some level interactive.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/07/20 alle ore 00:21:14