Affordable Access

Publisher Website

Metal ion complexation and folding of linear peptides

Authors
Journal
Biophysical Chemistry
0301-4622
Publisher
Elsevier
Publication Date
Volume
97
Issue
1
Identifiers
DOI: 10.1016/s0301-4622(02)00041-8
Keywords
  • Peptide-Metal Complex
  • Nmr
  • Nickel
  • Protein Folding
Disciplines
  • Medicine

Abstract

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) 3GASYQDLG(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.

There are no comments yet on this publication. Be the first to share your thoughts.

Statistics

Seen <100 times
0 Comments

More articles like this

Metal ion complexation and folding of linear pepti...

on Biophysical Chemistry May 23, 2002

Nanopore analysis of the effect of metal ions on t...

on Protein and peptide letters March 2014

Complexation of sulfur containing aminoacids and p...

on Inorganica Chimica Acta Jan 01, 1983

Aromatic donor-acceptor charge-transfer and metal-...

on Angewandte Chemie Internationa... Jun 21, 2004
More articles like this..