The conformational preferences of proteinogenic glutamic acid esterified (GluOMe) and N-acetylated (Ac-GluOMe) derivatives have been determined in solution for the first time. Theoretical calculations at the ωB97X-D/aug-cc-pVTZ made possible the assignment of six and eight stable conformers for GluOMe and AcGluOMe, respectively. The conformational equilibrium of the studied compounds was evaluated in different organic solvents using a combination of the integral equation formalism polarizable continuum model (IEF-PCM) and 1 H NMR spectroscopy data. The results showed that the conformational equilibrium of both derivatives change in the presence of solvent. According to the quantum theory of atoms in molecules (QTAIM), non-covalent interactions (NCI), and natural bond orbitals (NBO) analyses, the conformational preferences observed for GluOMe and AcGluOMe are not dictated by the presence of a specific interaction but are due to a combination of hyperconjugative and steric effects.
Revealing the Conformational Preferences of Proteinogenic Glutamic Acid Derivatives in Solution by 1 H NMR Spectroscopy and Theoretical Calculations
Posted by
Weslley G. D. P. Silva
on 12 09 2019
Related content
19 04 2023
< 1 minute
Predicting pKa
One of the most important physicochemical properties of small molecules and macromolecules are the...
12 05 2022
< 1 minute
Coupling stabilizers open KV1-type potassium channels
ABSTRACT: The opening and closing of voltage-gated ion channels are regulated by voltage sensors...
12 11 2021
< 1 minute
Responding to the Challenge Posed by the Generic Control of Substances
Drug monitoring organizations report that new psychoactive substances continue to emerge, posing...
12 10 2021
< 1 minute
Boost analytical experiments with phys-chem properties
Physicochemical properties have a fundamental impact on analytical experiment conditions,...