High Resolution Nmr Data of 8-Deoxy-Lactucin

1983 ◽  
Vol 46 (2) ◽  
pp. 277-278 ◽  
Author(s):  
Giuseppe Savona ◽  
Maurizio Bruno
2017 ◽  
Vol 55 (8) ◽  
pp. 738-746 ◽  
Author(s):  
Vadim Zorin ◽  
Michael A. Bernstein ◽  
Carlos Cobas

2017 ◽  
Vol 282 ◽  
pp. 62-70 ◽  
Author(s):  
Elias Aboutanios ◽  
Donald S. Thomas ◽  
James M. Hook ◽  
Carlos Cobas

2008 ◽  
Vol 86 (12) ◽  
pp. 1077-1084 ◽  
Author(s):  
Marie-Rose Van Calsteren ◽  
Christopher K Jankowski ◽  
Ricardo Reyes-Chilpa ◽  
Manuel Jiménez-Estrada ◽  
Maria G Campos ◽  
...  

The structure and stereochemistry of four sesquiterpene lactones, budlein A (1), zaluzanin A (2), and glaucolides D (3a) and E (3b), isolated from Mexican Asteraceae species, for which only partial NMR data could be found in the literature, were determined. A combination of 1D and 2D high-resolution NMR experiments, such as DEPT, COSY, NOESY, ROESY, HMQC, HSQC, and HMBC, were used to completely assign the 1H and 13C spectra. The crystal structures of zaluzanin A (2) and glaucolide E (3b) were also determined. Glaucolides D and E have been previously reported to relax KCl-induced contraction in rat uterine smooth muscle; therefore, the effects of zaluzanin A and budlein A were examined in the same model. It was found that both compounds can relax contraction induced by KCl, but only zaluzanin A induced relaxation when contraction was induced with oxytocin. The preliminary biological test results according to these profiles are reported in this paper.Key words: NMR data, X-ray data, sesquiterpene lactones, Mexican Asteraceae, smooth muscle relaxant.


2013 ◽  
Vol 450 (2) ◽  
pp. 321-332 ◽  
Author(s):  
Nader T. Amin ◽  
A. Katrine Wallis ◽  
Stephen A. Wells ◽  
Michelle L. Rowe ◽  
Richard A. Williamson ◽  
...  

ERp27 (endoplasmic reticulum protein 27.7 kDa) is a homologue of PDI (protein disulfide-isomerase) localized to the endoplasmic reticulum. ERp27 is predicted to consist of two thioredoxin-fold domains homologous with the non-catalytic b and b′ domains of PDI. The structure in solution of the N-terminal b-like domain of ERp27 was solved using high-resolution NMR data. The structure confirms that it has the thioredoxin fold and that ERp27 is a member of the PDI family. 15N-NMR relaxation data were obtained and ModelFree analysis highlighted limited exchange contributions and slow internal motions, and indicated that the domain has an average order parameter S2 of 0.79. Comparison of the single-domain structure determined in the present study with the equivalent domain within full-length ERp27, determined independently by X-ray diffraction, indicated very close agreement. The domain interface inferred from NMR data in solution was much more extensive than that observed in the X-ray structure, suggesting that the domains flex independently and that crystallization selects one specific interdomain orientation. This led us to apply a new rapid method to simulate the flexibility of the full-length protein, establishing that the domains show considerable freedom to flex (tilt and twist) about the interdomain linker, consistent with the NMR data.


1969 ◽  
Vol 52 (5) ◽  
pp. 1074-1092 ◽  
Author(s):  
L H Keith ◽  
A L Alford ◽  
A W Garrison

Abstract The high resolution nuclear magnetic resonance spectra of the DDT class of pesticides and related compounds are discussed, including a study of the resonances of the aromatic protons as they are affected by various substiluents. The CCl3 moiety on the α-carbon strongly deshields the ortho protons on the aromatic rings, and this deshielding effect is greatly enhanced by substitution of a chlorine ortho rather than para on the aromatic ring. These deshielding effects are explained by a consideration of the electronegativity of the substituents and the stereochemistry of the molecule. The chemical shifts and coupling constants are tabulated.


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