NMR and dielectric spectroscopy investigation of protein dynamical structure.
β Scribed by V.D. Fedotov; Yu.D. Feldman; A.G. Krushelnitsky; I.V. Ermolina
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 317 KB
- Volume
- 219
- Category
- Article
- ISSN
- 0022-2860
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The DNA-binding protein HU from Bacillus stearothermophilus (HUBst) is a dimer with a molecular weight of 195 kDa that is capable of bending DNA. An x-ray structure has been determined previously [Tanaka et al. 1984) Nature, vol. 310, pp. 376-381], but no structure could be established for a large p
## Abstract Tritium nmr spectroscopy of specifically tritiated tosylchymotrypsin has been used to examine the properties of the tosyl group in this protein. The unavoidable presence of several tritiated isotopomers complicates analysis of experiments and extensive computer simulations of relaxation