The conformational behavior of a heterodetic bicyclic decapeptide (BCPLT) in the absence and in the presence of calcium ions has been studied by means of mono and two-dimensional nmr techniques. Free BCPLT possesses a quite compact structure stabilized by intramolecular bonds and turns. In the structure a cluster of carbonyls is located in a cavity that is supposed to be the cation binding site.
BICYCLIC PEPTIDES - SOLUTION CONFORMATION AND CA-2+ BINDING OF THE HETERODETIC BICYCLIC DECAPEPTIDE CYCLO(GLU1-LEU2-PRO3-GLY4-SER5-ILE6-PRO7-ALA8)-CYCLO(1-GAMMA- 5-BETA) PHE9-GLY10 / Zanotti, G.; Pinnen, F.; Lucente, G.; Paolillo, Livio; D'Auria, Gabriella; Trivellone, E.; D'Alagni, M.. - In: BIOPOLYMERS. - ISSN 0006-3525. - STAMPA. - 28:1(1989), pp. 305-317. [10.1002/bip.360280131]
BICYCLIC PEPTIDES - SOLUTION CONFORMATION AND CA-2+ BINDING OF THE HETERODETIC BICYCLIC DECAPEPTIDE CYCLO(GLU1-LEU2-PRO3-GLY4-SER5-ILE6-PRO7-ALA8)-CYCLO(1-GAMMA- 5-BETA) PHE9-GLY10
PAOLILLO, LIVIO;D'AURIA, GABRIELLA;
1989
Abstract
The conformational behavior of a heterodetic bicyclic decapeptide (BCPLT) in the absence and in the presence of calcium ions has been studied by means of mono and two-dimensional nmr techniques. Free BCPLT possesses a quite compact structure stabilized by intramolecular bonds and turns. In the structure a cluster of carbonyls is located in a cavity that is supposed to be the cation binding site.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
