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001-es BibID:	BIBFORM019087
Első szerző:	Jószai Viktória (vegyész)
Cím:	Palladium(II) complexes of oligopeptides containing aspartyl and glutamyl residues / Viktória Jószai, Imre Sóvágó
Dátum:	2011
ISSN:	0277-5387
Megjegyzések:	Potentiometric and 1H NMR spectroscopic measurements have been performed on palladium(II) complexes of di-, tri- and tetra-peptides containing aspartyl and glutamyl residues including AspAla, AlaAsp, AspAsp, AspAspAsp, GluGluGlu, GlyAspGly, AspAspAspAsp and GlyGlyAspGly. In the case of dipeptides the coordination modes are basically determined by the peptide backbone. The presence of the extra b-carboxylate residues does not result in new binding modes but these functions may slightly affect the thermodynamic stability of several species. For tripeptides the most important findings are connected to the governing role of the b-carboxylate group of internal aspartyl residues but similar effects were not observed for the peptides containing glutamic acid. Aspartic acid in the second position of a tripeptide (Xaa-Asp-Yaa sequence) promotes the binding of the preceding and prevents deprotonation and coordination of subsequent amide functions. In the case of tetrapeptides, the aspartyl residues present in the third position from the N-terminus (Xaa-Yaa-Asp-Zaa sequence) have the most pronounced effect on complex formation. In this case, the (NH2, N, N, b-COO)-coordination is the major binding mode and the species [PdH 2L] can exist in a wide pH range. The enhanced
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Palladium Peptides Aspartic acid Glutamic acid Potentiometry Stability constants NMR spectroscopy
Megjelenés:	Polyhedron. - 30 : 12 (2011), p. 2114-2120. -
További szerzők:	Sóvágó Imre (1946-) (vegyész)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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