Measurements have been made of the proton NMR spin-lattice relaxation at 60,30 and 18 MHZ in solid ribonudwse A from IO to 300 K. and in a-chymotrypsin, lysozyme and deuterated lysozyme from 120 to 300 K. Reorientation of the methyl groups is the predominant moIecular motion causing relaxation. A lo
The role of water in the dynamics and proton relaxation of solid proteins
β Scribed by E.R. Andrew; D.J. Bryant; T.Z. Rizvi
- Publisher
- Elsevier Science
- Year
- 1983
- Tongue
- English
- Weight
- 413 KB
- Volume
- 95
- Category
- Article
- ISSN
- 0009-2614
No coin nor oath required. For personal study only.
β¦ Synopsis
The effect of progessive hydration up to 60% by weight of Hz0 and D20 on the proton relasation of polycrystalline achymotrypsin and lysozyme has been examined. The dynamical behaviour of the protein molecules was not affected by hydration. The dynamics of the water molecules was characterized. and the activation energy of successive increments was found to decrease.
π SIMILAR VOLUMES
## Synopsis Spin-spin and spin-lattice 'H-nmr relaxation times of the sea anemone polypeptide anthopleurin-A were measured at frequencies of 200, 300, 400, and 500 MHz. Relaxation times were fitted iteratively by least squares regression to the isotropic tumbling model, Woessner's model for anisot
We studied a dynamical model for the motion of the large scales of proteins in water. The model was obtained by projecting the (averaged) Newton equations onto some set of harmonic modes. We compared the statistics of the so-obtained trajectories with those obtained by standard techniques, and concl