The tetrapeptide Z-Leu-Aib-Pro-Val-OBg monohydrate.
The intramolecular hydrogen-bonding pattern of Z-Leu-Aib-Pro-Val-OBg monohydrate [(N-benzhydrylamino)carbonylmethyl N-benzyloxycarbonyl-alpha-aminoisobutyrylprolylvalinate monohydrate], C(43)H(55)N(5)O(8).H(2)O, is unusual for a tetrapeptide because, in addition to a 1-->4 hydrogen bond, a second hydrogen bond of the type 1-->5 is formed. This folding reflects the intramolecular hydrogen-bonding pattern that this amino acid sequence adopts in the naturally occurring peptaibol alamethicin.
Gessmann
Renate
R
IMBB/FORTH, PO Box 1527, 71110 Iraklion, Crete, Greece. rege777@yahoo.com
Schiemann
Norbert
N
Brückner
Hans
H
Petratos
Kyriacos
K
D006860:Hydrogen Bonding; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry*; D011487:Protein Conformation
D009842:Oligopeptides