The heteronuclear NMR relaxation of globular proteins depends on the anisotropic rotational diffusion tensor. Using our previous developments for prediction of hydrodynamic properties of arbitrarily shaped particles, by means of bead models, we have constructed a computational procedure to calculate
✦ LIBER ✦
Efficient, Accurate Calculation of Rotational Diffusion and NMR Relaxation of Globular Proteins from Atomic-Level Structures and Approximate Hydrodynamic Calculations
✍ Scribed by Ortega, Alvaro; García de la Torre, Jose
- Book ID
- 126293722
- Publisher
- American Chemical Society
- Year
- 2005
- Tongue
- English
- Weight
- 79 KB
- Volume
- 127
- Category
- Article
- ISSN
- 0002-7863
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
HYDRONMR: Prediction of NMR Relaxation o
✍
J Garcı́a de la Torre; M.L Huertas; B Carrasco
📂
Article
📅
2000
🏛
Elsevier Science
🌐
English
⚖ 189 KB
Protein NMR Techniques Volume 278 || Cha
✍
Downing, A. Kristina
📂
Article
📅
2004
🏛
Humana Press
🌐
English
⚖ 654 KB
This Second Edition Of Protein Nmr Techniques Is Well Written With A Dynamic Approach That Covers Multiple Topics Within Its Nineteen Chapters. The Text Opens With A Review Of Recombinant Protein Expression Using Two Organisms, E. Coli And P. Pastoris That Can Produce High Yields Of Isotopically Lab