Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/4656
Title: Metal ion complexation and folding of linear peptides.
Authors: Spiga, Ottavia 
Scarselli, M
Bernini, Andrea 
Ciutti, A
Giovannoni, L
Laschi, Franco 
Bracci, Luisa
Niccolai, Neri 
Issue Date: 2002
Project: None 
Journal: BIOPHYSICAL CHEMISTRY
Abstract: 
A Linear peptide, GASYQDLG was synthesised and used as a model to evaluate the effects of nickel additions to increase the conformational stability. The NMR data obtained for the peptide and its histidyl derivative (H)(3)GASYQDLG(H)(3) suggest that in solution folded structures are present only for the H-tagged peptide-Ni(II) ion system. These results suggest that metal ions and additions of a double histidine tags of suitable length can be used as efficient tools to reduce peptide flexibility without other internal modifications. Synthesis of H-tagged analogs could offer a promising strategy for large-scale preparation of diagnostic tools and, in general, whenever more rigid molecular structures should be advisable.
Description: 
36896
URI: http://hdl.handle.net/20.500.12779/4656
ISSN: 0301-4622
DOI: 10.1016/S0301-4622(02)00041-8
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