2 results match your criteria: "University of Toronto UTM[Affiliation]"
Characterization of conformational states of the homodimeric enzyme fluoroacetate dehalogenase by F-C two-dimensional NMR.
RSC Chem Biol
October 2024
Department of Chemistry, University of Toronto UTM, 3359 Mississauga Rd Mississauga ON Canada L5L 1C6
Article Synopsis
- Tryptophan is vital for protein stability and function, with researchers using fluorine nuclear magnetic resonance (NMR) to study its dynamics and interactions in proteins.
- By incorporating fluorinated tryptophan analogs during protein expression, scientists can explore how these modified residues affect protein behavior and structure.
- The study specifically focuses on the enzyme fluoroacetate dehalogenase, using advanced NMR techniques to analyze the roles of tryptophan residues in allosteric communication and binding interactions.
Nuts and Bolts of CF3 and CH 3 NMR Toward the Understanding of Conformational Exchange of GPCRs.
Methods Mol Biol
May 2016
Department of Chemistry, University of Toronto (UTM), 3359 Mississauga Road North, Mississauga, ON, Canada, L5L 1C6,
With the advent of efficient protein expression and functional purification protocols, it is now possible to reconstitute many G protein-coupled receptors (GPCRs) in detergent micelles at concentrations of 25 μM or more. Such concentrations are sufficient for studies of conformational states and dynamics relating to function and the mechanism of activation of GPCRs, using solution state NMR. In particular, methyl spectroscopy, in the form of one-dimensional (19)F NMR or two-dimensional ((1)H,(13)C) NMR, provides high fidelity spectra which reveal detailed features associated with conformational states and their lifetimes, as a function of ligand.
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