Photo-CIDNP NMR Spectroscopy of Amino Acids and Proteins

Author(s):  
Lars T. Kuhn
Keyword(s):  
2003 ◽  
Vol 42 (4) ◽  
pp. 1006-1013 ◽  
Author(s):  
Judith Bravo ◽  
Carlos Cativiela ◽  
Julio E. Chaves ◽  
Rafael Navarro ◽  
Esteban P. Urriolabeitia

Author(s):  
Hanchang Zhang ◽  
Hongmei Zhao ◽  
Jie Wen ◽  
Zhanbin Zhang ◽  
Pericles Stavropoulos ◽  
...  

Enantiomers of a few new amides containing two stereogenic centers have been derived from D- and L-α-amino acids as guests for chiral recognition by 1H NMR spectroscopy. A variety of...


Foods ◽  
2020 ◽  
Vol 9 (10) ◽  
pp. 1436
Author(s):  
Yang Soo Byeon ◽  
Dabeen Lee ◽  
Young-Shick Hong ◽  
Seung-Taik Lim ◽  
Sang Sook Kim ◽  
...  

The objective of this study was to compare the physicochemical, enzymatic, and metabolic properties of two control wheat malts imported from Germany and the US to those of malts made from three Korean wheat varieties: Triticumaestivum L., var. Anzunbaengi, Jokyung, and Keumkang. The qualities and enzyme activities of the Korean wheat malts were generally similar to those of the control wheat malts. The Korean wheat malts had slightly lower diastatic power and enzyme activities related to saccharification. The analysis of metabolites in the wheat malt samples was performed using 1H nuclear magnetic resonance (NMR) metabolomics, which identified 32 metabolites that differed significantly among the samples. Most amino acids and lipids were more abundant in the Korean wheat malts than in the control wheat malts. These differences among malts could influence the quality and flavor of wheat beers. Further brewing studies are necessary to identify the association between beer quality and individual malt metabolites.


ChemPhysChem ◽  
2016 ◽  
Vol 17 (23) ◽  
pp. 4011-4027 ◽  
Author(s):  
Stanislav L. Veinberg ◽  
Zachary W. Friedl ◽  
Austin W. Lindquist ◽  
Brianna Kispal ◽  
Kristopher J. Harris ◽  
...  

2015 ◽  
Vol 13 (44) ◽  
pp. 10797-10801 ◽  
Author(s):  
Jordi Solà ◽  
Michael Bolte ◽  
Ignacio Alfonso

Oligomers made by click chemistry display a duality of secondary structures similar to natural peptides as inferred by NMR spectroscopy and X-ray diffraction experiments.


1971 ◽  
Vol 26 (3) ◽  
pp. 213-222 ◽  
Author(s):  
Wolfgang Voelter ◽  
Günther Jung ◽  
Eberhard Breitmaier ◽  
Ernst Bayer

Pulse - Fourier - Transform-13C-NMR spectroscopy allowed the direct recording of 13C-NMR spectra of amino acids and peptides with natural abundance of 13C isotopes within a reasonable time. The 13C-signals of more than 50 free and protected amino acids and several peptides were assigned. 13C-NMR spectroscopy gives valuable information about the carbon skeleton, thus offering a new analytical tool for the study of biopolymers and their constituents.


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