117709-92-9Relevant academic research and scientific papers
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
Determination of an 8-? interatomic distance in a helical peptide by solid-state NMR spectroscopy
Holl, Susan M.,Marshall, Garland R.,Beusen, Denise D.,Kociolek, Karol,Redlinski, Adam S.,Leplawy, Miroslaw T.,McKay, Robert A.,Vega, Shimon,Schaefer, Jacob
, p. 4830 - 4833 (2007/10/02)
The combination of transferred-echo double resonance (TEDOR) with rotational-echo double resonance (REDOR) has been used to measure an 8-? fluorine-carbon internuclear distance in a nine-residue fragment of the peptide antibiotic emerimicin. The fragment is 19FCH2CO-Phe-MeA-MeA-[1-13C]MeA-[ 15N]Val-Gly-Leu-MeA-MeA-OBzl (MeA = α-methylalanine or aminoisobutyric acid). The TEDOR part of this magic-angle-spinning, solid-state NMR experiment selects the 13C label by its dipolar coupling to 15N and suppresses the natural-abundance carbon background. The REDOR part of the experiment measures dipolar coupling of the selected carbon to 19F. The TEDOR-REDOR combined experiment works with a variety of spin 1/2 nuclei and can be used to characterize internuclear distances and geometry in macromolecular aggregates that do not crystallize.
