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...
[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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[NMR paper] Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.
Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR.
Biochemistry. 2021 Jan 05;:
Authors: Crilly CJ, Brom JA, Kowalewski ME, Piszkiewicz S, Pielak GJ
Abstract
Water is key to protein structure and stability, yet the relationship between protein-water interactions and...
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[ASAP] Dried Protein Structure Revealed at the Residue Level by Liquid-Observed Vapor Exchange NMR
Dried Protein Structure Revealed at the Residue Level 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.0c00863/20210105/images/medium/bi0c00863_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00863
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[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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[NMR paper] Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
Related Articles Water-protein hydrogen exchange in the micro-crystalline protein crh as observed by solid state NMR spectroscopy.
J Biomol NMR. 2005 Jul;32(3):195-207
Authors: Böckmann A, Juy M, Bettler E, Emsley L, Galinier A, Penin F, Lesage A
We report site-resolved observation of hydrogen exchange in the micro-crystalline protein Crh. Our approach is based on the use of proton T2' -selective 1H-13C-13C correlation spectra for...
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12-01-2010 06:56 PM
[NMR paper] NMR relaxation studies of the role of conformational entropy in protein stability and
NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Related Articles NMR relaxation studies of the role of conformational entropy in protein stability and ligand binding.
Acc Chem Res. 2001 May;34(5):379-88
Authors: Stone MJ
Recent advances in the measurement and analysis of protein NMR relaxation data have made it possible to characterize the dynamical properties of many backbone and side chain groups. With certain caveats, changes in flexibility that occur upon ligand binding, mutation, or...
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[NMR paper] Stability of beta-galactosidase, a model protein drug, is related to water mobility a
Stability of beta-galactosidase, a model protein drug, is related to water mobility as measured by 17O nuclear magnetic resonance (NMR).
Related Articles Stability of beta-galactosidase, a model protein drug, is related to water mobility as measured by 17O nuclear magnetic resonance (NMR).
Pharm Res. 1993 Jan;10(1):103-8
Authors: Yoshioka S, Aso Y, Izutsu K, Terao T
The inactivation of freeze-dried beta-galactosidase during storage was studied, focusing on the effect of water mobility as measured by the spin-lattice relaxation time, T1, of...
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[NMR paper] Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A s
Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A study of bovine serum albumin by diverse NMR techniques.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Fluctuations, exchange processes, and water diffusion in aqueous protein systems: A study of bovine serum albumin by diverse NMR techniques.
Biophys J. 1990 Nov;58(5):1183-97
Authors: Kimmich R, Gneiting T, Kotitschke K, Schnur G
Experimental frequency, concentration, and...