Determination of the Geographical Origin of Asparagus officinalis L. by 1H NMR Spectroscopy

2020 ◽  
Vol 68 (49) ◽  
pp. 14353-14363
Author(s):  
Juliane Klare ◽  
Marc Rurik ◽  
Eric Rottmann ◽  
Anke Bollen ◽  
Oliver Kohlbacher ◽  
...  
2018 ◽  
Vol 66 (44) ◽  
pp. 11873-11879 ◽  
Author(s):  
René Bachmann ◽  
Sven Klockmann ◽  
Johanna Haerdter ◽  
Markus Fischer ◽  
Thomas Hackl

2020 ◽  
Vol 68 (52) ◽  
pp. 15526-15534
Author(s):  
Caroline Schmitt ◽  
Tobias Schneider ◽  
Laura Rumask ◽  
Markus Fischer ◽  
Thomas Hackl

Molecules ◽  
2019 ◽  
Vol 24 (3) ◽  
pp. 405 ◽  
Author(s):  
Brett H. Pogostin ◽  
Anders Malmendal ◽  
Casey H. Londergan ◽  
Karin S. Åkerfeldt

Determining the pKa of key functional groups is critical to understanding the pH-dependent behavior of biological proteins and peptide-based biomaterials. Traditionally, 1H NMR spectroscopy has been used to determine the pKa of amino acids; however, for larger molecules and aggregating systems, this method can be practically impossible. Previous studies concluded that the C-D stretches in Raman are a useful alternative for determining the pKa of histidine residues. In this study, we report on the Raman application of the C2-D probe on histidine’s imidazole side chain to determining the pKa of histidine in a short peptide sequence. The pKa of the tripeptide was found via difference Raman spectroscopy to be 6.82, and this value was independently confirmed via 1H NMR spectroscopy on the same peptide. The C2-D probe was also compared to other Raman reporters of the protonation state of histidine and was determined to be more sensitive and reliable than other protonation-dependent signals. The C2-D Raman probe expands the tool box available to chemists interested in directly interrogating the pKa’s of histidine-containing peptide and protein systems.


2019 ◽  
Vol 91 (7) ◽  
pp. 4429-4435 ◽  
Author(s):  
Christopher L. Suiter ◽  
Mark O. McLinden ◽  
Thomas J. Bruno ◽  
Jason A. Widegren

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