𝔖 Bobbio Scriptorium
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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

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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-

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## 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

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## 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