[NMR paper] Protein Allostery Study in Cells Using NMR Spectroscopy
Protein Allostery Study in Cells Using NMR Spectroscopy
Protein allostery is commonly observed in vitro. But how protein allostery behaves in cells is unknown. In this work, a protein monomer-dimer equilibrium system was built with the allosteric effect on the binding characterized using NMR spectroscopy through mutations away from the dimer interface. A chemical shift linear fitting method was developed that enabled us to accurately determine the dissociation constant. A total of 28 allosteric mutations were prepared and grouped to negative...
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04-24-2024 05:58 AM
[NMR paper] NMR spectroscopy to study the fate of metallodrugs in cells
NMR spectroscopy to study the fate of metallodrugs in cells
Metal-based drugs can modulate various biological processes and exhibit a rich variety of properties that foster their use in biomedicine and chemical biology. On the way to intracellular targets, ligand exchange and redox reactions can take place, thus making metallodrug speciation in vivo a challenging task. Advances in NMR spectroscopy have made it possible to move from solution to live-cell studies and elucidate the transport of metallodrugs and interactions with macromolecular targets in a...
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04-23-2021 07:01 AM
[NMR paper] Relaxation dispersion NMR spectroscopy for the study of protein allostery.
Relaxation dispersion NMR spectroscopy for the study of protein allostery.
Related Articles Relaxation dispersion NMR spectroscopy for the study of protein allostery.
Biophys Rev. 2015 Jun;7(2):191-200
Authors: Farber PJ, Mittermaier A
Abstract
Allosteric transmission of information between distant sites in biological macromolecules often involves collective transitions between active and inactive conformations. Nuclear magnetic resonance (NMR) spectroscopy can yield detailed information on these dynamics. In particular,...
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05-18-2017 03:23 PM
[NMR paper] NMR Methods to Study Dynamic Allostery.
NMR Methods to Study Dynamic Allostery.
NMR Methods to Study Dynamic Allostery.
PLoS Comput Biol. 2016 Mar;12(3):e1004620
Authors: Grutsch S, Brüschweiler S, Tollinger M
Abstract
Nuclear magnetic resonance (NMR) spectroscopy provides a unique toolbox of experimental probes for studying dynamic processes on a wide range of timescales, ranging from picoseconds to milliseconds and beyond. Along with NMR hardware developments, recent methodological advancements have enabled the characterization of allosteric proteins at...
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03-11-2016 12:00 PM
[NMR paper] Solution NMR Spectroscopy for the Study of Enzyme Allostery.
Solution NMR Spectroscopy for the Study of Enzyme Allostery.
Related Articles Solution NMR Spectroscopy for the Study of Enzyme Allostery.
Chem Rev. 2016 Jan 6;
Authors: Lisi GP, Loria JP
Abstract
Allostery is a ubiquitous biological regulatory process in which distant binding sites within a protein or enzyme are functionally and thermodynamically coupled. Allosteric interactions play essential roles in many enzymological mechanisms, often facilitating formation of enzyme-substrate complexes and/or product release. Thus,...
Protein Allostery Study in Cells Using NMR Spectroscopy - ACS Publications
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