Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement [Chemistry]
Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement
Yusuke Okuno, Janghyun Yoo, Charles D. Schwieters, Robert B. Best, Hoi Sung Chung, G. Marius Clore...
Date: 2021-08-17
The cosolvent effect arises from the interaction of cosolute molecules with a protein and alters the equilibrium between native and unfolded states. Denaturants shift the equilibrium toward the latter, while osmolytes stabilize the former. The molecular mechanism whereby cosolutes perturb protein stability is still the subject of considerable debate....
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08-18-2021 11:11 AM
[NMR paper] Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement
Atomic view of cosolute-induced protein denaturation probed by NMR solvent paramagnetic relaxation enhancement
The cosolvent effect arises from the interaction of cosolute molecules with a protein and alters the equilibrium between native and unfolded states. Denaturants shift the equilibrium toward the latter, while osmolytes stabilize the former. The molecular mechanism whereby cosolutes perturb protein stability is still the subject of considerable debate. Probing the molecular details of the cosolvent effect is experimentally challenging as the interactions are very weak and transient,...
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08-18-2021 11:11 AM
High-pressure and cold denaturation
High-pressure and cold denaturation
High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin
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11-19-2016 08:35 PM
[NMR paper] Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of
Cold denaturation of barstar: 1H, 15N and 13C NMR assignment and characterisation of residual structure.
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Detection of residual structure in denatured proteins is of interest because fleetingly structured regions may be initiation points of the...
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08-22-2010 02:27 PM
[NMR paper] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
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Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range....
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08-21-2010 11:12 PM
[NMR paper] Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H N
Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Related Articles Cold denaturation and heat denaturation of Streptomyces subtilisin inhibitor. 2. 1H NMR studies.
Biochemistry. 1991 Nov 26;30(47):11313-20
Authors: Tamura A, Kimura K, Akasaka K
Structural transitions of the protein Streptomyces subtilisin inhibitor (SSI) from the native state to the cold-denatured and heat-denatured states were studied by 1H NMR spectroscopy in the temperature range from -10 to 60 degrees C in the acidic pH range....