Dodecapeptide Ac-Asp-Lys-Asp-Gly-Asn-Gly-Tyr-Ile-Ser-Ala-Ala-Gaba-OH [I, Gaba = NH(CH2)3CO] was prepd. by the solid phase method with a total protection scheme using PAM-resin. Purified I was characterized by 1H NMR spectroscopy, both in the presence and in the absence of calcium ions at various pH values. No strong specific interaction occurred between I and Ca2+ in aq. solns.
Modified calmodulin calcium binding domain III. Solid phase synthesis, purification and proton NMR characterization / Pavone, Vincenzo; Di Nola, A.; Andini, Salvatore; Ferrara, Luciano; Di Blasio, B.; Benedetti, Ettore; Pucci, Pietro. - In: INTERNATIONAL JOURNAL OF PEPTIDE & PROTEIN RESEARCH. - ISSN 0367-8377. - STAMPA. - 23:5(1984), pp. 454-461.
Modified calmodulin calcium binding domain III. Solid phase synthesis, purification and proton NMR characterization.
PAVONE, VINCENZO;ANDINI, SALVATORE;FERRARA, LUCIANO;BENEDETTI, ETTORE;PUCCI, PIETRO
1984
Abstract
Dodecapeptide Ac-Asp-Lys-Asp-Gly-Asn-Gly-Tyr-Ile-Ser-Ala-Ala-Gaba-OH [I, Gaba = NH(CH2)3CO] was prepd. by the solid phase method with a total protection scheme using PAM-resin. Purified I was characterized by 1H NMR spectroscopy, both in the presence and in the absence of calcium ions at various pH values. No strong specific interaction occurred between I and Ca2+ in aq. solns.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
