Related ArticlesNMR line shape analysis of a multi-state ligand binding mechanism in chitosanase.
J Biomol NMR. 2017 Apr 09;:
Authors: Shinya S, Ghinet MG, Brzezinski R, Furuita K, Kojima C, Shah S, Kovrigin EL, Fukamizo T
Abstract
Chitosan interaction with chitosanase was examined through analysis of spectral line shapes in the NMR HSQC titration experiments. We established that the substrate, chitosan hexamer, binds to the enzyme through the three-state induced-fit mechanism with fast formation of the encounter complex followed by slow isomerization of the bound-state into the final conformation. Mapping of the chemical shift perturbations in two sequential steps of the mechanism highlighted involvement of the substrate-binding subsites and the hinge region in the binding reaction. Equilibrium parameters of the three-state model agreed with the overall thermodynamic dissociation constant determined by ITC. This study presented the first kinetic evidence of the induced-fit mechanism in the glycoside hydrolases.
PMID: 28393280 [PubMed - as supplied by publisher]
NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase
NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase
Abstract
Chitosan interaction with chitosanase was examined through analysis of spectral line shapes in the NMR HSQC titration experiments. We established that the substrate, chitosan hexamer, binds to the enzyme through the three-state induced-fit mechanism with fast formation of the encounter complex followed by slow isomerization of the bound-state into the final conformation. Mapping of the chemical shift perturbations in two sequential steps of the mechanism...
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04-10-2017 12:51 AM
Ligand Binding Properties of the Lentil Lipid TransferProtein: Molecular Insight into the Possible Mechanism of Lipid Uptake
Ligand Binding Properties of the Lentil Lipid TransferProtein: Molecular Insight into the Possible Mechanism of Lipid Uptake
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01079/20170316/images/medium/bi-2016-010796_0006.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01079
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
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03-17-2017 08:02 AM
[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Related Articles Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
J Mass Spectrom. 2013 Aug;48(8):i
Authors: Santambrogio C, Favretto F, D'Onofrio M, Assfalg M, Grandori R, Molinari H
Abstract
Protein-ligand interactions are driven by many factors, including protein conformation and pH of the solution. Electrospray mass spectrometry can reveal the degree of protein folding from the distribution of...
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07-31-2013 12:00 PM
[NMR paper] Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
Mass spectrometry and NMR analysis of ligand binding by human liver fatty acid binding protein.
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J Mass Spectrom. 2013 Aug;48(8):895-903
Authors: Santambrogio C, Favretto F, D'Onofrio M, Assfalg M, Grandori R, Molinari H
Abstract
Human liver fatty acid binding protein (hL-FABP) is the most abundant cytosolic protein in the liver. This protein plays important roles associated to partitioning of fatty acids (FAs) to specific...
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07-31-2013 12:00 PM
NMR line shapes and multi-state binding equilibria
NMR line shapes and multi-state binding equilibria
Abstract Biological function of proteins relies on conformational transitions and binding of specific ligands. Proteinā??ligand interactions are thermodynamically and kinetically coupled to conformational changes in protein structures as conceptualized by the models of pre-existing equilibria and induced fit. NMR spectroscopy is particularly sensitive to complex ligand-binding modesā??NMR line-shape analysis can provide for thermodynamic and kinetic constants of ligand-binding equilibria with the site-specific resolution. However,...
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05-24-2012 05:54 AM
[NMR paper] Line shape considerations in ultrafast 2D NMR.
Line shape considerations in ultrafast 2D NMR.
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J Magn Reson. 2004 Feb;166(2):152-63
Authors: Shapira B, Lupulescu A, Shrot Y, Frydman L
We have recently proposed and demonstrated an approach that enables the acquisition of 2D nuclear magnetic resonance (NMR) spectra within a single scan. The approach is based on spatially encoding the spins' evolution along the indirect domain with the aid of a magnetic field gradient, and subsequently decoding this information numerous times over...
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11-24-2010 09:25 PM
[NMR paper] Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain fold
Dynamic NMR line-shape analysis demonstrates that the villin headpiece subdomain folds on the microsecond time scale.
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J Am Chem Soc. 2003 May 21;125(20):6032-3
Authors: Wang M, Tang Y, Sato S, Vugmeyster L, McKnight CJ, Raleigh DP
There is considerable interest in small proteins that fold very rapidly. These proteins have become attractive targets for both theoretical and computational studies. The...
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11-24-2010 09:01 PM
Insights into the Mechanism of Ligand Binding to Octopine Dehydrogenase from Pecten m
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PLoS One. 2010;5(8):
Authors: Smits SH, Meyer T, Mueller A, van Os N, Stoldt M, Willbold D, Schmitt L, Grieshaber MK
Octopine dehydrogenase (OcDH) from the adductor muscle of the great scallop, Pecten maximus, catalyzes the NADH dependent, reductive condensation of L-arginine and pyruvate to...
NMR line shape analysis of a multi-state ligand binding mechanism in chitosanase.
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