Long-Range Distance Measurements of Protein Binding Sites by Rotational-Echo Double-Resonance NMR
โ Scribed by Studelska, Daniel R.; Klug, Christopher A.; Beusen, Denise D.; McDowell, Lynda M.; Schaefer, Jacob
- Book ID
- 127290899
- Publisher
- American Chemical Society
- Year
- 1996
- Tongue
- English
- Weight
- 120 KB
- Volume
- 118
- Category
- Article
- ISSN
- 0002-7863
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
The utility of rotational echo double resonance REDOR NMR spectroscopy for determining the conformations of linear peptides has been examined critically using a series of crystalline and amorphous samples. The focus of the present work ห13 15 ## ลฝ . was the evaluation of long-distance ) 5 A inter
A method based on rotational-echo double-resonance (REDOR) NMR is proposed to measure 1 H-15 N bond lengths under magic-angle-spinning. Protons are selectively polarized and evolve under the frequency-switched Lee-Goldburg (FSLG) homonuclear decoupling, while two 15 N p pulses are applied to restore
## Abstract Distance determination in disordered systems by a fourโpulse double electronโelectron resonance method (DEER or PELDOR) is becoming increasingly popular because long distances (several nanometers) and their distributions can be measured. From the distance distributions eventual heteroge