[NMR paper] Studying protein stability in crowded environments by NMR
Studying protein stability in crowded environments by NMR
Most proteins perform their functions in crowded and complex cellular environments where weak interactions are ubiquitous between biomolecules. These complex environments can modulate the protein folding energy landscape and hence affect protein stability. NMR is a nondestructive and effective method to quantify the kinetics and equilibrium thermodynamic stability of proteins at an atomic level within crowded environments and living cells. Here, we review NMR methods that can be used to measure...
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[NMR paper] Protein-Cadmium Interactions in Crowded Biomolecular Environments Probed by In-cell and Lysate NMR Spectroscopy
Protein-Cadmium Interactions in Crowded Biomolecular Environments Probed by In-cell and Lysate NMR Spectroscopy
One of the mechanisms by which toxic metal ions interfere with cellular functions is ionic mimicry, where they bind to protein sites in lieu of native metals Ca ^(2+) and Zn ^(2+) . The influence of crowded intracellular environments on these interactions is not well understood. Here, we demonstrate the application of in-cell and lysate NMR spectroscopy to obtain atomic-level information on how a potent environmental toxin cadmium interacts with its protein targets. The...
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[NMR paper] All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.
All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.
Related Articles All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy.
Nat Commun. 2020 Nov 13;11(1):5760
Authors: Köhn B, Kovermann M
Abstract
The high density of macromolecules affecting proteins due to volume exclusion has been discussed in theory but numerous in vivo experiments cannot be sufficiently understood taking only pure entropic stabilization into account. Here, we show...
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11-17-2020 07:53 AM
[NMR paper] Insights into protein stability in cell lysate by 19F NMR spectroscopy.
Insights into protein stability in cell lysate by 19F NMR spectroscopy.
Related Articles Insights into protein stability in cell lysate by 19F NMR spectroscopy.
Chembiochem. 2020 Aug 12;:
Authors: Welte H, Kovermann M
Abstract
In living organisms, protein folding and function take place in an inhomogeneous, highly crowded environment possessing a concentration of diverse macromolecules of up to 400*g/L. It has been shown that the intracellular environment has a pronounced effect on the stability, dynamics and function of the...
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08-15-2020 05:51 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these interactions...
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09-30-2011 06:00 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
All atom insights into the impact of crowded environments on protein stability by NMR spectroscopy - Nature.com
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