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The Involvement of amino acid side chains in shielding the nickel coordination site: an NMR study

Medici, Serenella and Peana, Massimiliano Francesco and Nurchi, Valeria Marina and Zoroddu, Maria Antonietta (2013) The Involvement of amino acid side chains in shielding the nickel coordination site: an NMR study. Molecules, Vol. 18 (10), p. 12396-12414. eISSN 1420-3049. Article.

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DOI: 10.3390/molecules181012396

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Coordination of proteins and peptides to metal ions is known to affect their properties, often by a change in their structural organization. Side chains of the residues directly involved in metal binding or very close to the coordination centre may arrange themselves around it, in such a way that they can, for instance, disrupt the protein functions or stabilize a metal complex by shielding it from the attack of water or other small molecules. The conformation of these side chains may be crucial to different biological or toxic processes. In our research we have encountered such behaviour in several cases, leading to interesting results for our purposes. Here we give an overview on the structural changes involving peptide side chains induced by Ni(II) coordination. In this paper we deal with a number of peptides, deriving from proteins containing one or more metal coordinating sites, which have been studied through a series of NMR experiments in their structural changes caused by Ni(II) complexation. Several peptides have been included in the study: short sequences from serum albumin (HSA), Des-Angiotensinogen, the 30-amino acid tail of histone H4, some fragments from histone H2A and H2B, the initial fragment of human protamine HP2 and selected fragments from prion and Cap43 proteins. NMR was the election technique for gathering structural information. Experiments performed for this purpose included 1D ¹H and ¹³C, and 2D HSQC, COSY, TOCSY, NOESY and ROESY acquisitions, which allowed the calculation of the Ni(II) complexes structural models.

Item Type:Article
ID Code:9659
Uncontrolled Keywords:Nuclear magnetic resonance spectroscopy, NMR structure, structural models, nickel peptide complexes, amino acid side chains
Subjects:Area 03 - Scienze chimiche > CHIM/03 Chimica generale e inorganica
Divisions:001 Università di Sassari > 01-a Nuovi Dipartimenti dal 2012 > Chimica e Farmacia
Publisher:Molecular Diversity Preservation International
Copyright Holders:© 2013 by the authors; licensee MDPI; Basel, Switzerland
Deposited On:04 Mar 2014 09:28

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