values of torsion angles È and É show the presence of two type III 0 -turns, at the Á Z Phe 2 and Gly 3 residues, and Gly 3 and Á Z Phe 4 residues. All amino acids in the peptide are linked trans to each other. Two intramolecular N-HÁ Á ÁO hydrogen bonds, between CO and NH groups, stabilize -turns p
N-[tert-Butoxycarbonylglycyl-(E)-α,β-dehydrophenylalanylglycylglycyl-(E)-α,β-dehydrophenylalanyl]glycine
✍ Scribed by Makowski, Maciej ;Lisowski, Marek ;Mikołajczyk, Iwona ;Lis, Tadeusz
- Book ID
- 104488907
- Publisher
- International Union of Crystallography
- Year
- 2006
- Tongue
- English
- Weight
- 144 KB
- Volume
- 63
- Category
- Article
- ISSN
- 1600-5368
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📜 SIMILAR VOLUMES
Á2H 2 O, adopts the type I -turn conformation for the Á Z Phe 2 -Gly 3 residues. It is stabilized by a 4 ! 1 intramolecular hydrogen bond between the Á E Phe 4 NH and Gly 1 CO groups. All the amino acid residues in the pentapeptide sequence are linked trans to each other. The crystal structure is st
## Abstract The effect of cooling down to 150 K on the structures of __α__- (s.g. __P__2~1~/__n__), __β__- (s.g. __P__2~1~), and __γ__- (s.g. __P__3~1~) polymorphs of glycine was studied by X-ray single-crystal diffraction. No polymorphic transformations were detected. Relative volume changes and t