A comparison of Segmental Dynamics in Polymers by Solid-State 13C NMR Spectroscopy
β Scribed by McGrath, K. J.; Ngai, K. L.; Roland, C. M.
- Book ID
- 126285704
- Publisher
- American Chemical Society
- Year
- 1995
- Tongue
- English
- Weight
- 712 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0024-9297
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Solid-state nuclear magnetic resonance spectroscopy was used to study the motion of 2H and 19F probes attached to the skeletal muscle actin residues Cys-lO, Lys-61 and Cys-374. The probe resonances were observed in dried and hydrated G-actin, F-actin and F-actin-myosin subfragment-1 complexes. Restr
## Ε½ . 2 Recent two-dimensional 2D H-NMR studies on nearly ideal mixtures are reviewed. The use of selective deuterium labeling allows the unambiguous observation of the individual segmental dynamics of each component in the blend. 2D exchange spectra provide both the mean motional rates and the m