Version 2 2020-03-20, 19:42Version 2 2020-03-20, 19:42
Version 1 2020-03-19, 21:43Version 1 2020-03-19, 21:43
journal contribution
posted on 2020-03-20, 19:42authored byRio Febrian, William J. Ona, Juan F. Araneda, Susanne D. Riegel, Paul J. Bracher
This Article describes a method that
increases the chemical shift
dispersion of signals in proton nuclear magnetic resonance (1H NMR) spectra of peptides
by the addition of salts to the sample. We demonstrate that the addition
of potassium phosphate to aliquots of reactions of glycine peptides
permits the measurement of their rate constants for hydrolysis by
a 60 MHz benchtop instrument, which would otherwise be infeasible
due to overlapping signals in the salt-free mixtures. The method is
described in detail and validated by comparison to analysis on a 400
MHz spectrometer. The ability to use benchtop NMR spectroscopy to
study reactions of simple peptides enables interested scientists at
a broader array of institutionsnot just those institutions
capable of affording high-field NMR instrumentsto participate
in original research projects like those aimed at elucidating the
chemistry that led to the origin of life on Earth.