| Autor: |
Yagi H; Research School of Chemistry, Australian National University, Canberra, ACT, 0200, Australia., Loscha KV, Su XC, Stanton-Cook M, Huber T, Otting G |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of biomolecular NMR [J Biomol NMR] 2010 Jun; Vol. 47 (2), pp. 143-53. Date of Electronic Publication: 2010 Apr 20. |
| DOI: |
10.1007/s10858-010-9416-x |
| Abstrakt: |
Paramagnetic relaxation enhancements (PRE) present a powerful source of structural information in nuclear magnetic resonance (NMR) studies of proteins and protein-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)](3-), 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)](3-) to protein, allowing quantitative distance measurements for nuclear spins within about 15 A of the Gd(3+) ion. Such data accurately define the metal position relative to the protein, greatly enhancing the interpretation of pseudocontact shifts induced by [Ln(DPA)(3)](3-) complexes of paramagnetic lanthanide (Ln(3+)) ions other than gadolinium. As an example we studied the quaternary structure of the homodimeric GCN4 leucine zipper. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
|
Full text from SpringerLink