CD-n.m.r. study of the solution conformation of bradykinin analogs containing α-aminoisobutyric acid
✍ Scribed by CANN, JOHN R. ;LONDON, ROBERT E. ;UNKEFER, CLIFFORD J. ;VAVREK, RAYMOND J. ;STEWART, JOHN M.
- Book ID
- 115098609
- Publisher
- Wiley (Blackwell Publishing)
- Year
- 2009
- Tongue
- English
- Weight
- 704 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0367-8377
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📜 SIMILAR VOLUMES
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-
## 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
Amylose (average d.p. 1000) and amylodextrin (average d.p. 25) have identical 13C-n.m.r. spectra, except for some minor signals from the small amount of (u-1+6 branch linkages present in amylodextrin. Amylodextrin can be obtained as stable solutions in much higher concentrations than amylose and so