## Abstract The sideβchain dynamics of solid polylysine at various hydration levels was studied by means of proton spinβlattice relaxation times measurements in the laboratory and tilted (offβresonance) rotating frames at several temperatures as well as Monte Carlo computer simulations. These data
Leucine Side-Chain Conformation and Dynamics in Proteins from 13C NMR Chemical Shifts
β Scribed by Frans A. A. Mulder
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 211 KB
- Volume
- 10
- Category
- Article
- ISSN
- 1439-4227
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