## Abstract The side‐chain dynamics of solid polylysine at various hydration levels was studied by means of proton spin–lattice relaxation times measurements in the laboratory and tilted (off‐resonance) rotating frames at several temperatures as well as Monte Carlo computer simulations. These data
1H-NMR study of water dynamics in hydrated collagen: Transverse relaxation-time and diffusion analysis
✍ Scribed by A. Traore; L. Foucat; J. P. Renou
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2000
- Tongue
- English
- Weight
- 131 KB
- Volume
- 53
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Water proton transverse relaxation times (T 2 ) and self-diffusion coefficients (D) were measured in randomly oriented hydrated collagen fibers. Three T 2 relaxation times were discerned indicating the presence of at least three water fractions in the collagen sample. The D values associated with each water fraction were determined. The diffusion time dependence of D suggests water motion is restricted by macromolecular structure. The experimental results are discussed with reference to the structural properties of hydrated collagen fibers.
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