[NMR paper] Visualizing an Allosteric Intermediate Using CuAAC Stabilization of an NMR Mixed Labeled Dimer
Visualizing an Allosteric Intermediate Using CuAAC Stabilization of an NMR Mixed Labeled Dimer
Homodimers are the most abundant type of enzyme in cells, and as such, they represent the most elemental system for studying the phenomenon of allostery. In these systems, in which the allosteric features are manifest by the effect of the first binding event on a similar event at the second site, the most informative state is the asymmetric singly bound (lig(1)) form, yet it tends to be thermodynamically elusive. Here we obtain milligram quantities of lig(1) of the allosteric homodimer,...
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[NMR paper] Mixed Fluorotryptophan Substitutions at the Same Residue Expand the Versatility of ｹ?F Protein NMR Spectroscopy.
Mixed Fluorotryptophan Substitutions at the Same Residue Expand the Versatility of ｹ?F Protein NMR Spectroscopy.
Mixed Fluorotryptophan Substitutions at the Same Residue Expand the Versatility of ｹ?F Protein NMR Spectroscopy.
Chemistry. 2018 Jan 17;:
Authors: Kenward C, Shin K, Rainey J
Abstract
The strategy of applying fluorine NMR to characterize ligand binding to a membrane protein prepared with mixtures of tryptophans substituted with F at different positions on the indole ring was tested. The ｹ?F NMR behavior of 4-, 5-, 6-,...
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[NMR paper] Insulin allosteric behavior: detection, identification, and quantification of alloste
Insulin allosteric behavior: detection, identification, and quantification of allosteric states via 19F NMR.
Related Articles Insulin allosteric behavior: detection, identification, and quantification of allosteric states via 19F NMR.
Biochemistry. 2005 May 31;44(21):7656-68
Authors: Bonaccio M, Ghaderi N, Borchardt D, Dunn MF
The insulin hexamer is an allosteric protein widely used in formulations for the treatment of diabetes. The hexamer exhibits positive and negative cooperativity and apparent half-site binding activity, reflecting the...
Mixed, nonclassical behavior in a classic allosteric protein ... - pnas.org
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