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1

Department of Chemistry and Pharmacy, University of Sassari, Via Vienna 2, 07100, Sassari, Italy

2

Department of Chemical and Geological Sciences, University of Cagliari, Cittadella Universitaria, I-09042 Monserrato, Cagliari, Italy





*

Author to whom correspondence should be addressed.



Abstract 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 NiII 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 NiII 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 NiII complexes structural models. View Full-Text

Keywords: nuclear magnetic resonance spectroscopy; NMR structure; structural models; nickel peptide complexes; amino acid side chains nuclear magnetic resonance spectroscopy; NMR structure; structural models; nickel peptide complexes; amino acid side chains





Author: Serenella Medici 1, Massimiliano Peana 1, Valeria Marina Nurchi 2 and Maria Antonietta Zoroddu 1,*

Source: http://mdpi.com/



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