Protein effective rotational correlation times from translational self-diffusion coefficients measured by PFG-NMR
- Author(s)
- Yao, S; Babon, JJ; Norton, RS;
- Details
- Publication Year 2008-08,Volume 136,Issue #2-3,Page 145-151
- Journal Title
- BIOPHYSICAL CHEMISTRY
- Publication Type
- Journal Article
- Abstract
- Molecular rotational correlation times are of interest for many studies carried out in solution, including characterization of biomolecular structure and interactions. Here we have evaluated the estimates of protein effective rotational correlation times from their translational self-diffusion coefficients measured by pulsedfield gradient NMR against correlation times determined from both collective and residue-specific 15 N relaxation analyses and those derived from 3D structure-based hydrodynamic calculations. The results show that, provided the protein diffusive behavior is coherent with the Debye-Stokes-Einstein model, translational diffusion coefficients provide rapid estimates with reasonable accuracy of their effective rotational correlation times. Effective rotational correlation times estimated from translational diffusion coefficients may be particularly beneficial in cases where i) isotopically labelled material is not available, ii) collective backbone (15)N relaxation rates are difficult to interpret because of the presence of flexible termini or loops, or iii) a full relaxation analysis is practically difficult because of limited sensitivity owing to low protein concentration, high molecular mass or low temperatures. (c) 2008 Elsevier B.V. All rights reserved.
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- SOLVENT VISCOSITIES; BACKBONE DYNAMICS; N-15 RELAXATION; SPECTROSCOPY; AGGREGATION; ASSOCIATION; UBIQUITIN; BINDING; DOMAIN
- Publisher's Version
- https://doi.org/10.1016/j.bpc.2008.06.002
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 2008-08-01 12:00:00