Tunable paramagnetic relaxation enhancements by [Gd(DPA)3]3â?? for protein structure

[nmrlearner]

Abstract Paramagnetic relaxation enhancements (PRE) present a powerful source of structural information in nuclear magnetic resonance (NMR) studies of proteins and proteinâ??ligand complexes. In contrast to conventional PRE reagents that are covalently attached to the protein, the complex between gadolinium and three dipicolinic acid (DPA) molecules, [Gd(DPA)3]3â??, can bind to proteins in a non-covalent yet site-specific manner. This offers straightforward access to PREs that can be scaled by using different ratios of [Gd(DPA)3]3â?? to protein, allowing quantitative distance measurements for nuclear spins within about 15 Ã? of the Gd3+ ion. Such data accurately define the metal position relative to the protein, greatly enhancing the interpretation of pseudocontact shifts induced by [Ln(DPA)3]3â?? complexes of paramagnetic lanthanide (Ln3+) ions other than gadolinium. As an example we studied the quaternary structure of the homodimeric GCN4 leucine zipper.

• Content Type Journal Article
• DOI 10.1007/s10858-010-9416-x
• Authors
  • Hiromasa Yagi, Australian National University Research School of Chemistry Canberra ACT 0200 Australia
  • Karin V. Loscha, Australian National University Research School of Chemistry Canberra ACT 0200 Australia
  • Xun-Cheng Su, Australian National University Research School of Chemistry Canberra ACT 0200 Australia
  • Mitchell Stanton-Cook, University of Queensland School of Chemistry and Molecular Biosciences Brisbane QLD 4072 Australia
  • Thomas Huber, University of Queensland School of Chemistry and Molecular Biosciences Brisbane QLD 4072 Australia
  • Gottfried Otting, Australian National University Research School of Chemistry Canberra ACT 0200 Australia

• • Journal Journal of Biomolecular NMR
  • Online ISSN 1573-5001
  • Print ISSN 0925-2738
  • Journal Volume Volume 47
  • Journal Issue Volume 47, Number 2

Source: Journal of Biomolecular NMR