Identification of a Conserved Histidine As Being Criticalfor the Catalytic Mechanism and Functional Switching of the MultifunctionalProline Utilization A Protein
Identification of a Conserved Histidine As Being Criticalfor the Catalytic Mechanism and Functional Switching of the MultifunctionalProline Utilization A Protein
[NMR paper] A Combined Utilization of (1)H NMR, IR and Theoretical Calculations to Elucidate the Conformational Preferences of Some L-Histidine Derivatives.
A Combined Utilization of (1)H NMR, IR and Theoretical Calculations to Elucidate the Conformational Preferences of Some L-Histidine Derivatives.
A Combined Utilization of (1)H NMR, IR and Theoretical Calculations to Elucidate the Conformational Preferences of Some L-Histidine Derivatives.
J Phys Chem A. 2017 Jan 04;:
Authors: Braga CB, Rittner R
Abstract
The conformational preferences of amino acids and their derivatives have been subject of many investigations, since protein folding pathways that determine tridimensional...
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[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
Abstract
Enzymatic synthesis...
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NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
NMR Detection of pH-Dependent Histidine–Water Proton Exchange Reveals the Conduction Mechanism of a Transmembrane Proton Channel
Fanghao Hu, Klaus Schmidt-Rohr and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2081185/aop/images/medium/ja-2011-081185_0008.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2081185
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/C3pPoB5_PR8
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10-22-2011 10:16 AM
[NMR paper] The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic
The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis.
Related Articles The roles of active-site residues in the catalytic mechanism of trans-3-chloroacrylic acid dehalogenase: a kinetic, NMR, and mutational analysis.
Biochemistry. 2004 Apr 13;43(14):4082-91
Authors: Azurmendi HF, Wang SC, Massiah MA, Poelarends GJ, Whitman CP, Mildvan AS
trans-3-Chloroacrylic acid dehalogenase (CaaD) converts trans-3-chloroacrylic acid to malonate semialdehyde by the...
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11-24-2010 09:51 PM
[NMR paper] NMR investigation of the catalytic mechanism of arylamine N-acetyltransferase from Sa
NMR investigation of the catalytic mechanism of arylamine N-acetyltransferase from Salmonella typhimurium.
Related Articles NMR investigation of the catalytic mechanism of arylamine N-acetyltransferase from Salmonella typhimurium.
Biochim Biophys Acta. 2003 Mar 17;1620(1-3):8-14
Authors: Delgoda R, Lian LY, Sandy J, Sim E
Arylamine N-acetyltransferases (NAT) are a family of enzymes found in both eucaryotes and procaryotes, which catalyse the N-acetylation of a range of arylamine and hydrazine drugs and carcinogenic arylamines, using acetyl...
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[NMR paper] Identification by NMR of the binding surface for the histidine-containing phosphocarr
Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
Biochemistry. 1997 Apr 15;36(15):4393-8
Authors: Garrett DS, Seok YJ,...
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08-22-2010 03:31 PM
[NMR paper] Identification by NMR of the binding surface for the histidine-containing phosphocarr
Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system.
Biochemistry. 1997 Apr 15;36(15):4393-8
Authors: Garrett DS, Seok YJ,...
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[NMR paper] Identification of the C2-1H histidine NMR resonances in chloramphenicol acetyltransfe
Identification of the C2-1H histidine NMR resonances in chloramphenicol acetyltransferase by a 13C-1H heteronuclear multiple quantum coherence method.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Identification of the C2-1H histidine NMR resonances in chloramphenicol acetyltransferase by a 13C-1H heteronuclear multiple quantum coherence method.
FEBS Lett. 1991 Mar 11;280(1):125-8
Authors: Derrick JP, Lian LY, Roberts GC, Shaw WV
Chloramphenicol acetyltransferase...
Identification of a Conserved Histidine As Being Criticalfor the Catalytic Mechanism and Functional Switching of the MultifunctionalProline Utilization A Protein
Linear Mode
