## Abstract The ^13^C NMR spectra for Lโlysine hydrochloride dihydrate are reported for static samples and samples spinning at the magic angle, which provide resolution of each carbon resonance. The spectra and the __T__~1s~, __T__~1p~ and __T__~1~ relaxation times for the carbon atoms demonstrate
The hydration response of poly(L-lysine) dynamics measured by 13C-nmr spectroscopy
โ Scribed by Scott D. Swanson; Robert G. Bryant
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1991
- Tongue
- English
- Weight
- 552 KB
- Volume
- 31
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
โฆ Synopsis
SYNOPSIS
'.'C-nmr measurements are reported for samples of poly (L-lysine) both static and spinning a t the magic angle in the @-sheet form as a function of water content. T h e addition of water decreases the side-chain line widths considerably. Measurements of the cross-polarization time constants indicate that hydration by either H 2 0 or D 2 0 increases the time constant. Measurements of spin-lattice relaxation times in the laboratory frame and the rotating frame indicate t h a t hydration does not change the dynamics of the backbone carbon atoms in the P-sheet structure appreciably, but the side-chain atoms experience considerable increase in local mobility with increasing hydration. Deuteration of the exchangeable protons or the water has only small effects on the carbon relaxation times, indicating t h a t relaxation is driven by intramolecular dipole-dipole interactions.
๐ SIMILAR VOLUMES
## Abstract The rates at which a peptide hexamer and a peptide octamer interconvert between leftโ and rightโhanded helical forms in CD~2~Cl~2~ solution have been characterized by ^13^C dynamic NMR (DNMR) spectroscopy. The peptide esters studied are Fmocโ(Aib)~__n__~โOtBu (__n__ = 6 and 8), where Fm
[guanidino-13C]Creatine has been synthesized by reaction involving synthesis of [13C]cyanamide followed by its condensation with sarcosine. The creatine guanidino carbon 13C NMR frequency shifts upon the formation of phosphocreatine by 0.83 ppm with a splitting (2JCP = 3.3 Hz) due to two-bond phosph
## Abstract This article describes a solidโstate NMR (SSNMR) investigation of the influence of hydration and chemical crossโlinking on the molecular dynamics of the constituents of the bovine pericardium (BP) tissues and its relation to the mechanical properties of the tissue. Samples of natural ph