Please use this identifier to cite or link to this item:
|Title:||Metal ion complexation and folding of linear peptides.||Authors:||Spiga, Ottavia
|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.
|Appears in Collections:||Publications|
Show full item record
checked on May 8, 2021
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.