Some theoretical studies have predicted that the conformational freedom of the cy-aminoisobutyric acid (H-Aib-OH) residue is restricted to the a-helical region of the Ramachandran map. In order to obtain conformational experimental data, two model peptide derivatives, MeCO-Aib-NHMe 1 and Bu'CO-LPro-
H N.M.R. STUDIES OF PROTECTED α-AMINOISOBUTYRIC ACID CONTAINING PEPTIDES
✍ Scribed by IQBAL, M. ;NAGARAJ, R. ;BALARAM, P.
- Book ID
- 115097770
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 379 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0367-8377
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Boc‐Gly‐L‐Ala‐Aib‐OMe (**1**) crystallizes in the space group __P__2~1~2~1~2~1~ with __a__ = 10.043(3), __b__ = 11.590(5), __c__ = 16.779(1) Å, and __Z__ = 4 (__R__ value for 1859 symmetry independent reflexions: 0.043). On the basis of a 4 → 1 intramolecular hydrogen bond, the tripepti
## Abstract The CD spectra of the peptides Boc‐X‐(Aib‐X)~__n__~‐OMe (__n__ = 1, 2, 3) and Boc‐(Aib‐X)~5~‐OMe, where X = L‐Ala or L‐Val have been examined in several solvents. The X = Ala and Val peptides behave similarly in all solvents, suggesting that the Aib residues dominate the folding prefere