Structure of benzyloxycarbonyl-l-alanyl-α-aminoisobutyric acid, Z-l-Ala-Aib-OH
✍ Scribed by Taga, T. ;Itoh, M. ;Machida, K. ;Fujita, T. ;Ichihara, T.
- Book ID
- 114506585
- Publisher
- International Union of Crystallography
- Year
- 1989
- Tongue
- English
- Weight
- 329 KB
- Volume
- 45
- Category
- Article
- ISSN
- 0108-2701
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## Abstract The x‐ray diffraction study of the C‐terminally unprotected tripeptide benzyloxycarbonyl‐L‐alanyl‐α‐aminoisobutyl‐α‐aminoisobutylic acid (Z‐L‐Ala‐Aib‐Aib‐OH) has shown that the molecule adopts a consecutive type III β‐turn, which characterizes a right‐handed 3~10~ helix. A very weak 4 →
## 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 crystal and molecular structures of two α‐aminoisobutyric acid (Aib)‐containing diketopiperazines, cyclo(Aib‐Aib) 1 and cyclo(Aib‐L‐Ile) **2**, are reported. Cyclo(Aib‐Aib) crystallizes in the space group P1 with __a__ = 5.649(3), __b__ = 5.865(2), __c__ = 8.363(1), α = 69.89(6), β
## Abstract The x‐ray structure of Boc‐L‐Ala‐Aib‐Ala‐Aib‐Ala‐Glu(OBzl)‐Ala‐Aib‐Ala‐Aib‐Ala‐OMe(I) represents the first α‐helix determined by direct methods. This undecapeptide is a model of the N‐terminus of alamethicin, and it exhibits voltage‐dependent pores in bilayer membranes at a higher volta