Deuterium Quadrupole-Coupling and Chemical-Shielding Tensors in the Model Dipeptide Glycylglycine Monohydrochloride Monohydrate
✍ Scribed by Carl A. Michal; J.Christopher Wehman; Lynn W. Jelinski
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 189 KB
- Volume
- 111
- Category
- Article
- ISSN
- 1064-1866
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✦ Synopsis
The electric field gradient (EFG) and chemical-shift (CS) tenhave been few full CS determinations for the peptide group sors for the amide, carboxylic acid, and amino deuteron sites in , carboxyl CS tensors are well represented in the literglycylglycine monohydrochloride monohydrate were measured. ature ( ) . For each site, the EFG tensors are found to lie nearly along the In this paper, we present EFG and chemical-shift tensors deuteron bond. The magnitudes of the quadrupole-coupling confor all the exchangeable deuteron sites in the model dipeptide stants agree well with previous empirical relationships to hydroglycylglycine monohydrochloride monohydrate: gen-bond lengths. A new relationship is presented which correlates hydrogen-bonding geometries and EFG asymmetry parameters for N-Drrr (hydrogen-bond acceptor) systems that suggests the importance of intermolecular geometry in determining these parameters. The measured amino and amide CS tensors are found to agree well with the few examples in the literature and agree qualitatively with those determined from ab initio calculations. The carboxylic acid deuteron CS tensor agrees well with empirical relationships to hydrogen-bond distance.