Protein Backbone 15N Relaxation Rates as a Tool for the Diagnosis of Structure Quality
✍ Scribed by Eva de Alba; Nico Tjandra
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 59 KB
- Volume
- 144
- Category
- Article
- ISSN
- 1090-7807
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✦ Synopsis
In the work reported herein we define a structure validation factor that depends on protein backbone 15 N relaxation rates. This is an alternative method to the previously defined quality factors derived from anisotropic chemical shifts or residual dipolar couplings. We have used the structure dependence of 15 N relaxation rates of anisotropically tumbling proteins to calculate this structure diagnosis factor and have used it to demonstrate the improvement of protein structures refined with residual dipolar couplings.
📜 SIMILAR VOLUMES
The magnitude of the quadrupole coupling constant (e2Qq/h) of a deuteron is a good probe for hydrogen bonding. In protein structures, hydrogen-bonding interactions between side chains, between side chaings and ligands, and between side chains and solvent are frequently found. An experiment that dete
## Abstract Relaxation times, __T__, due to the dipolar mechanism of relaxation of ^31^P nuclei were determined for eight pairs of 1,3‐dithianes with P‐containing substituents at the anomeric carbon atom. The separation of dipole–dipole from the total spin–lattice relaxation could be applied for th