## Abstract The molecular mechanism of thermal unfolding of yeast tRNA^Phe^ in 20 mM NaCl, 1 m__M__ EDTA, and 10 m__M__ MgSO~4~, pH 7.1 Β± 0.1, has been examined by ^31^P magnetic relaxation and the nuclear Overhauser effect methods at 40.48 MHz in the temperature range of 22.5β80Β°C. Two partially r
Simulation of proton spin-lattice relaxation times of yeast transfer RNAPhe
β Scribed by Fumikazu Hayashi; Susumu Shibata; Kazuyuki Akasaka; Hiroyuki Hatano
- Publisher
- Elsevier Science
- Year
- 1977
- Weight
- 521 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0022-2364
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π SIMILAR VOLUMES
The magnetic field dependence of the water-proton spin-lattice relaxation rate (1/T(1)) in tissues results from magnetic coupling to the protons of the rotationally immobilized components of the tissue. As a consequence, the magnetic field dependence of the water-proton (1/T(1)) is a scaled report o
On binding of gadolinium ions to the terminal carboxyl group of a peptide, the spin-lattice relaxation times of the WC protons are reduced sequentially from the C terminus, thus allowing the sequence determination of submilligram amounts of peptides.
In vivo spin-lattice relaxation times (TI) of water and lipid protons were measured in normal and dystrophic chicken pectoralis muscles at different ages. Values were obtained with a surface coil used as both a receiver and a transmitter. A 28-TI-8-Acquisition sequence was used for these measurments