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Correction: Perspectives on the Origin of Biological Homochirality on Earth.
J Mol Evol
December 2024
Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijuku, Katsushika-Ku, Tokyo, 125-8585, Japan.
Assignment of the absolute configuration of molecules that are chiral by virtue of deuterium substitution using chiral tag molecular rotational resonance spectroscopy.
Chirality
November 2023
Department of Chemistry, University of Virginia, Charlottesville, Virginia, USA.
Chiral tag molecular rotational resonance (MRR) spectroscopy is used to assign the absolute configuration of molecules that are chiral by virtue of deuterium substitution. Interest in the improved performance of deuterated active pharmaceutical ingredients has led to the development of precision deuteration reactions. These reactions often generate enantioisotopomer reaction products that pose challenges for chiral analysis.
View Article and Find Full Text PDFDesign principles and functional basis of enantioselectivity of alanyl-tRNA synthetase and a chiral proofreader during protein biosynthesis.
Nucleic Acids Res
April 2023
CSIR-Centre for Cellular and Molecular Biology (CSIR-CCMB), Hyderabad, Telangana 500007, India.
Article Synopsis
- The study investigates how the cellular translation system maintains homochirality (preference for L-amino acids) in proteins, emphasizing the role of enzymes like alanyl-tRNA synthetase (AlaRS).
- It challenges previous models by demonstrating that AlaRS does not activate D-alanine and that its editing domain mainly corrects errors for other amino acids, not D-alanine.
- The research provides biochemical evidence for chiral specificity, reinforcing that the recognition mechanisms ensure accurate protein synthesis and uphold the L-chiral bias in amino acids.
Comparative QM/MM study on the inhibition mechanism of β-Hydroxynorvaline to Threonyl-tRNA synthetase.
J Mol Graph Model
September 2022
Department of Chemistry and Biochemistry, University of Windsor, Windsor, Ontario, N9B 3P4, Canada.
β-Hydroxynorvaline (βHNV) is unnatural amino acid structurally identical to the threonine amino acid with branched ethyl group instead of threonine's methyl. It is a known competitive inhibitor that readily bind to Threonyl-tRNA synthetase's (ThrRS) catalytic site and blocks its function. In this work, we utilized a combination of Molecular Dynamics simulation (MD) and Quantum Mechanics/Molecular Mechanics (QM/MM) methodologies to provide mechanistic insights into its inhibition reaction for ThrRS.
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