Structure-taste relationship of some sweet-tasting dipeptide esters
✍ Scribed by Leo B. P. Brussel; Hein G. Peer; Arnold van der Heijden
- Book ID
- 112541000
- Publisher
- Springer
- Year
- 1975
- Tongue
- English
- Weight
- 465 KB
- Volume
- 159
- Category
- Article
- ISSN
- 0044-3026
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📜 SIMILAR VOLUMES
## Abstract In order to investigate the conformational preferences to elicit tastes, conformational free energy calculations using an empirical potential (ECEPP/2) and the hydration shell model were carried out on the L‐aspartyl dipeptide methyl esters, L‐^+^HAsp^−^‐L‐Xaa‐OMe, in the hydrated state
## Abstract The synthesis and X‐ray diffraction analysis of two dipeptide taste ligands have been carried out as part of our study of the molecular basis of taste. The compounds L‐aspartyl‐D‐α‐methylphenylalanine methyl ester [L‐Asp‐D‐(αMe)Phe‐OMe] and L‐aspartyl‐D‐alanyl‐2,2,5,5‐tetramethylcyclope
The molecular basis of sweet taste was investigated by carrying out the crystal state conformational analysis by X-ray diffraction of the following dipeptide taste ligands: N-3,3-dimethylbutyl-aspartylphenylalanine methyl ester, I (N-DMB-Asp-Phe-OMe), its sodium salt (N-DMB-Asp-Phe-ONa), II, asparty