CONFORMATIONAL ANALYSIS OF CYCLO (L-CYSTINE
β Scribed by Mitra, Alok K. ;Chandrasekaran, R.
- Book ID
- 118701183
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 345 KB
- Volume
- 10
- Category
- Article
- ISSN
- 0367-8377
No coin nor oath required. For personal study only.
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## Abstract The E~0~ rotamer of __c__βGlyβMet has been found to be almost as equally populated as the F rotamer at low temperatures, whereas in __c__βGlyβD,LβNle and __c__βGlyβD,LβNvl the F rotamer predominates. The increase of the E~0~ rotamer population parallels the increase of the boat diketopi
## Abstract Cyclodipeptides containing LβThr and LβHis residues have been studied by ^1^H NMR in D~2~O and DMSOβ__d__~6~. In the neutral form in D~2~O as in DMSOβ__d__~6~, the folded form of the LβHis residue is not unique. The diketopiperazine ring seems to be not strictly planar.
## Abstract Empirical energy calculations on __cyclo__(LβProβLβPhe) and __cyclo__(LβProβDβPhe) indicate that different conformations are possible for each molecule. The theoretical results are compared to ir, nmr, and crystallographic data. The interdependence between diketopiperazine ring and side