Fourier transform proton NMR spectroscopy in aqueous solution
β Scribed by F.W Benz; J Feeney; G.C.K Roberts
- Publisher
- Elsevier Science
- Year
- 1972
- Weight
- 555 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0022-2364
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Proton magnetic resonance spectra of 5β²AMP were taken in the concentration range of 0.001β2.2__M__. The concentration profiles of __all__ the nonexchangeable protons were determined. The data for 5β²AMP was compared to those of adenine, adenosine, and poly(A). Theoretically computed isos
Modern protein Fourier transform infrared (FT-IR) spectroscopy has proven to be a versatile and sensitive technique, applicable to many aspects of protein characterization. The major practical drawback for the FT-IR spectroscopy of proteins is the large absorbance band of water, which overlaps the a
Dextran, glycogen, hydroxyethyl starch, and maltodextrin were derivatized with acrylic acid glycidyl ester at alkaline pH. The degree of derivatization was determined by water-elimination Fourier transform nuclear magnetic resonance (NMR) and compared with a bmmination method. The signals from the a
are always less than the corresponding valence energy. A spectral analysis of the band system, which, in the case of reactions Mo(CO), + H and Mo(CO), + N, occurs at 5200 A, indicates the presence of P-1 1' ~~ -59.75 -59.95 -60.45 -69.25 -69.90 -71.05 -71.20 -73.00 -73.75 -74.10 -74.60 -75.35 -75.80