[ASAP] Water’s Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR
Water’s Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.1c00552/20211001/images/medium/bi1c00552_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.1c00552
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10-02-2021 06:00 AM
[NMR paper] Water's Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR
Water's Variable Role in Protein Stability Uncovered by Liquid-Observed Vapor Exchange NMR
Water is essential to protein structure and stability, yet our understanding of how water shapes proteins is far from thorough. Our incomplete knowledge of protein-water interactions is due in part to a long-standing technological inability to assess experimentally how water removal impacts local protein structure. It is now possible to obtain residue-level information on dehydrated protein structures via liquid-observed vapor exchange (LOVE) NMR, a solution NMR technique that quantifies the...
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10-02-2021 06:00 AM
Essential Role of the Linker Region in the HigherCatalytic Efficiency of a Bifunctional MsrA–MsrB Fusion Protein
Essential Role of the Linker Region in the HigherCatalytic Efficiency of a Bifunctional MsrA–MsrB Fusion Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00544/20160901/images/medium/bi-2016-005445_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00544
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09-01-2016 07:21 PM
Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
Mechanism of the Flavoprotein l-HydroxynicotineOxidase: Kinetic Mechanism, Substrate Specificity, Reaction Product,and Roles of Active-Site Residues
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01325/20160115/images/medium/bi-2015-01325p_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01325
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01-16-2016 04:41 AM
[NMR paper] The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.
The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.
Related Articles The role of water in protein's behavior: The two dynamical crossovers studied by NMR and FTIR techniques.
Comput Struct Biotechnol J. 2015;13:33-7
Authors: Mallamace F, Corsaro C, Mallamace D, Vasi S, Vasi C, Dugo G
Abstract
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03-10-2015 07:22 PM
[NMR paper] Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Catalytic mechanism of ?-phosphate attack in dUTPase is revealed by X-ray crystallographic snapshots of distinct intermediates, 31P-NMR spectroscopy and reaction path modelling.
Nucleic Acids Res. 2013 Aug 27;
Authors: Barabás O, Németh V, Bodor A, Perczel A, Rosta E, Kele Z, Zagyva I, Szabadka Z, Grolmusz VI, Wilmanns M, Vértessy BG
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Enzymatic synthesis...
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08-29-2013 01:53 PM
[NMR paper] Protein hydration and location of water molecules in oxidized horse heart cytochrome
Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.
Related Articles Protein hydration and location of water molecules in oxidized horse heart cytochrome c by (1)H NMR.
J Magn Reson. 2000 Nov;147(1):1-8
Authors: Bertini I, Huber JG, Luchinat C, Piccioli M
The hydration properties of the oxidized form of horse heart cytochrome c have been studied by (1)H NMR spectroscopy. Two-dimensional, homonuclear ePHOGSY-NOESY experiments are used to map water-protein interactions. The detected NOEs reveal...