82527-04-6Relevant academic research and scientific papers
Crystallographic characterization of helical secondary structures in 2:1and 1:2 α/Β-peptides
Choi, Soo Hyuk,Guzei, Ilia A.,Spencer, Lara C.,Gellman, Samuel H.
supporting information; experimental part, p. 2917 - 2924 (2009/07/30)
Oligomers containing both α- and β-amino acid residues ("α/β-peptides") are intriguing as potential foldamers. A large setof α/β-peptide backbones can be generated by combining &alph a; and β-amino acid residues in different patterns; however, most resear
Emerimicins III and IV and their ethylalanine12 epimers. Facilitated chemical-enzymatic synthesis and a qualitative evaluation of their solution structures
Slomczynska, Urszula,Beusen, Denise D.,Zabrocki, Janusz,Kociolek, Karol,Redlinski, Adam,Rensser, Fritz,Hutton, William C.,Leplawy, Miroslaw T.,Marshall, Garland R.
, p. 4095 - 4106 (2007/10/02)
The peptaibol antibiotics, emerimicin III and IV (Ac-Phe1-MeA2-MeA3-MeA4-VaI 5-Gly6-Leu7-MeA8-MeA 9-Hyp10-Gln11-R-EtA12-Hyp
