[NMR paper] Enzyme Dynamics from NMR Spectroscopy.
Enzyme Dynamics from NMR Spectroscopy.
Enzyme Dynamics from NMR Spectroscopy.
Acc Chem Res. 2015 Jan 9;
Authors: Palmer AG
Abstract
Conspectus Biological activities of enzymes, including regulation or coordination of mechanistic stages preceding or following the chemical step, may depend upon kinetic or equilibrium changes in protein conformations. Exchange of more open or flexible conformational states with more closed or constrained states can influence inhibition, allosteric regulation, substrate recognition, formation of the...
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01-13-2015 02:31 PM
[NMR paper] A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
Related Articles A novel 2-oxoindolinylidene inhibitor of bacterial MurD ligase: Enzyme kinetics, protein-inhibitor binding by NMR and a molecular dynamics study.
Eur J Med Chem. 2014 Jun 11;83C:92-101
Authors: Sim?i? M, Pureber K, Kristan K, Urleb U, Kocjan D, Grdadolnik SG
Abstract
N-(5-(5-nitro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)4-oxo-2-thioxo-1,3-thiazolidin-3-yl)nicotinamide,...
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06-22-2014 12:24 PM
A Novel 2-oxoindolinylidene Inhibitor of Bacterial MurD Ligase: Enzyme Kinetics, Protein-Inhibitor Binding by NMR and a Molecular Dynamics Study
A Novel 2-oxoindolinylidene Inhibitor of Bacterial MurD Ligase: Enzyme Kinetics, Protein-Inhibitor Binding by NMR and a Molecular Dynamics Study
Publication date: Available online 11 June 2014
Source:European Journal of Medicinal Chemistry</br>
Author(s): Mihael Sim?i? , Kaja Pureber , Katja Kristan , Uroš Urleb , Darko Kocjan , Simona Goli? Grdadolnik</br>
N-(5-(5-nitro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)4-oxo-2-thioxo-1,3-thiazolidin-3-yl)nicotinamide, an 2-oxoindolinylidene derivative with novel structure scaffold, was evaluated for inhibition potency...
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06-12-2014 10:52 PM
[NMR paper] Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view.
Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Evolution of the concept of conformational dynamics of enzyme functions over half of a century: A personal view.
Biopolymers. 2013 Apr;99(4):263-9
Authors: Závodszky P, Hajdú I
Abstract
To most physicists, it was always evident that conformational fluctuation is an inherent...
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02-03-2013 10:19 AM
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin [Biophysics and Computational Biology]
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin
Struts, A. V., Salgado, G. F. J., Brown, M. F....
Date: 2011-05-17
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state 2H NMR relaxation allows investigation of light-induced changes in local ps–ns time scale motions of retinal bound to rhodopsin. Site-specific 2H labels were introduced into methyl groups of the...
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05-17-2011 08:40 PM
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Solid-state 2H NMR relaxation illuminates functional dynamics of retinal cofactor in membrane activation of rhodopsin.
Proc Natl Acad Sci U S A. 2011 Apr 28;
Authors: Struts AV, Salgado GF, Brown MF
Rhodopsin is a canonical member of the family of G protein-coupled receptors, which transmit signals across cellular membranes and are linked to many drug interventions in humans. Here we show that solid-state (2)H NMR relaxation...
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04-30-2011 12:36 PM
[NMR paper] 13C-NMR of Clostridium pasteurianum ferredoxin after reductive methylation of the ami
13C-NMR of Clostridium pasteurianum ferredoxin after reductive methylation of the amines using formaldehyde.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 13C-NMR of Clostridium pasteurianum ferredoxin after reductive methylation of the amines using formaldehyde.
Biochim Biophys Acta. 1990 Apr 19;1038(2):146-51
Authors: Gluck M, Sweeney WV
Clostridium pasteurianum 2(4Fe-4S) ferredoxin has been reductively methylated using formaldehyde and sodium cyanoborohydride....
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08-21-2010 10:48 PM
NMR post-doc position: NMR-based dynamics study of enzyme mechanism
The following post-doc position in NMR is available in University of Missouri:
Ad text:
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We have an opening for a postdoctoral fellow to use NMR to study dynamics of an enzyme while it is carrying on reversible catalysis. The prospects are promising and can be compared with thorough enzymology and crystallography of its ligand-dependent conformational changes (done in our dept.). The enzyme is sizeable enough to be challenging, but we have a battery of excellent 800 MHz spectra of deuterated samples for launching the project. The postdoctoral fellow will be housed in a new...