Various strategies are described and compared for measurement of one-bond J(NH) and J(NC') splittings in larger proteins. In order to evaluate the inherent resolution obtainable in the various experiments, relaxation rates of (15)N-(1)H(N) coupled and heteronuclear decoupled resonances were measured
Distinguishing the Effects of Cross Correlation and J Coupling in COSY Spectra of Paramagnetic Proteins
β Scribed by J. Qin; F. Delaglio; G.N. Lamar; A. Bax
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 372 KB
- Volume
- 102
- Category
- Article
- ISSN
- 1064-1866
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
A new experimental mixing scheme for band-selective Hartmann-Hahn transfer between the \(\mathrm{H}^{\mathrm{N}}\) and \(\mathrm{H}_{\alpha}\) resonances of peptides and proteins is presented. This form of tailored correlation spectroscopy (TACSY) allows enhancement of the sensitivity of specific (
We present a simple method for extracting interference effects between chemical shift anisotropy (CSA) and dipolar coupling from spin relaxation measurements in macromolecules, and we apply this method to extracting cross-correlation rates involving interference of amide 15N CSA and 15N-1H dipolar c
## Abstract The proton chemical shifts are reported for monosubstituted naphthalenes, quinolines and quinoxalines. Together with literature data, these chemical shifts are compared with the parent compounds and substituent effects evaluated statistically. The effect of substituents parallels that i