The Chemical Nature of Hydrogen Bonding in Proteins via NMR: J -Couplings, Chemical Shifts, and AIM Theory
โ Scribed by Arnold, William D.; Oldfield, Eric
- Book ID
- 120277826
- Publisher
- American Chemical Society
- Year
- 2000
- Tongue
- English
- Weight
- 85 KB
- Volume
- 122
- Category
- Article
- ISSN
- 0002-7863
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
## Abstract The change in ^1^H NMR chemical shifts upon hydrogen bonding was investigated using both experimental and theoretical methods. The ^1^H NMR spectra of a number of phenols were recorded in CDCl~3~ and DMSO solvents. For phenol, 2โ and 4โcyanophenol and 2โnitrophenol the OH chemical shift
## Abstract Internucleotide ^2h^__J__~NN~ spinโspin couplings and chemical shifts (ฮด(^1^H) and ฮฮด(^15^N)) of N๏ฃฟHยทยทยทN Hโbond units in the natural and radiationโdamaged GโC base pairs were predicted using the appropriate density functional theory calculations with a large basis set. Four possible ser