Tyrosine-glycine revisited : resolving the discrepancy between theory and experiment
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Energies of 20 conformers of the Tyr-Gly dipeptide were computed using DSD-PBEP86-D3BJ/aug-cc-VTZ, with geometries from M06-2X/6-31+G* and B97-D/6-31+G*. At 0 K, these energies support the earlier finding from MP2/6-31+G*//B3LYP/6-31+G*, that the most stable conformer is folded and H-bonded. However, when free-energy corrections at 400 K are added, non-H-bonded conformers are the most stable. This supports an earlier spectroscopic study in which H-bonded conformers were absent. Of the four most stable conformers at 400 K, two were not matched with spectra in the experimental study, but we argue that all four can in fact be plausibly assigned to the experimental spectra.
Holroyd , L F & van Mourik , T 2015 , ' Tyrosine-glycine revisited : resolving the discrepancy between theory and experiment ' Chemical Physics Letters , vol 621 , pp. 124-129 . DOI: 10.1016/j.cplett.2014.12.055
Chemical Physics Letters
Copyright © 2015 Published by Elsevier B.V. NOTICE: this is the author’s version of a work that was accepted for publication in Chemical Physics Letters. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Chemical Physics Letters (2015), doi:10.1016/j.cplett.2014.12.055
LFH acknowledges the Engineering and Physical Sciences Research Council for studentship support through the Doctoral Training Account scheme.
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