Newly identified C–H⋯ O hydrogen bond in histidine
RM Steinert, C Kasireddy, ME Heikes… - Physical Chemistry …, 2022 - pubs.rsc.org
New Cδ–H⋯ O histidine hydrogen bonding interactions in various proteins are identified by
neutron diffraction and computationally characterized. Neutron diffraction data shows …
neutron diffraction and computationally characterized. Neutron diffraction data shows …
Progress in our understanding of 19F chemical shifts
Fluorine NMR spectroscopy has diverse applications, including characterization of chemical
reaction mechanisms, protein structure–function studies, and solid-state NMR …
reaction mechanisms, protein structure–function studies, and solid-state NMR …
Evaluating electronic structure methods for accurate calculation of 19F chemical shifts in fluorinated amino acids
The ability of electronic structure methods (11 density functionals, HF, and MP2 calculations;
two basis sets and two solvation models) to accurately calculate the 19F chemical shifts of …
two basis sets and two solvation models) to accurately calculate the 19F chemical shifts of …
Analysis of Multiple Protein Alignments Using 3D-Structural Information on the Orientation of Amino Acid Side-Chains
DS Timonina, DA Suplatov - Molecular Biology, 2022 - Springer
Multiple alignment of amino acid sequences of homologous proteins is a key tool in state-of-
the-art bioinformatics and evolutionary analysis. Differences in the spatial orientation of …
the-art bioinformatics and evolutionary analysis. Differences in the spatial orientation of …
The biophysical probes 2-fluorohistidine and 4-fluorohistidine: spectroscopic signatures and molecular properties
Fluorinated amino acids serve as valuable biological probes, by reporting on local protein
structure and dynamics through 19F NMR chemical shifts. 2-fluorohistidine and 4 …
structure and dynamics through 19F NMR chemical shifts. 2-fluorohistidine and 4 …