[NMR paper] A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.
A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.
Related Articles A STD-NMR study of the interaction of the Anabaena ferredoxin-NADP+ reductase with the coenzyme.
Molecules. 2014;19(1):672-85
Authors: Antonini LV, Peregrina JR, Angulo J, Medina M, Nieto PM
Abstract
Ferredoxin-NADP+ reductase (FNR) catalyzes the electron transfer from ferredoxin to NADP+ via its flavin FAD cofactor. To get further insights in the architecture of the transient complexes produced during the...
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09-23-2014 01:57 PM
[NMR paper] Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
Related Articles Nmr structural studies of the first catalytic half-domain of ubiquitin activating enzyme.
J Struct Biol. 2013 Nov 6;
Authors: Jaremko M, Jaremko L, Nowakowski M, Wojciechowski M, Szczepanowski RH, Panecka R, Zhukov I, Bochtler M, Ejchart A
Abstract
We report a high resolution NMR structure and (15)N relaxation studies of the first catalytic cysteine half-domain (FCCH) of the mouse ubiquitin-activating enzyme E1, together with...
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11-12-2013 03:52 PM
[NMR paper] Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.rsc.org-images-entities-char_z_RSClogo.gif Related Articles Structural characterization of a peptoid with lysine-like side chains and biological activity using NMR and computational methods.
Org Biomol Chem. 2013 Jan 28;11(4):640-7
Authors: Sternberg U, Birtalan E, Jakovkin I, Luy B, Schepers U, Bräse S, Muhle-Goll C
Abstract
...
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06-05-2013 06:53 PM
NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein.
NMR characterizations of the ice binding surface of an antifreeze protein.
PLoS One. 2010;5(12):e15682
Authors: Hong J, Hu Y, Li C, Jia Z, Xia B, Jin C
Antifreeze protein (AFP) has a unique function of reducing solution freezing temperature to protect organisms from ice damage. However, its functional mechanism is not well understood. An intriguing question concerning AFP function is how the high selectivity for ice ligand is achieved in the presence of free water of...
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01-07-2011 11:21 PM
[NMR paper] Relation of enzyme activity to local/global stability of murine adenosine deaminase:
Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies.
Related Articles Relation of enzyme activity to local/global stability of murine adenosine deaminase: 19F NMR studies.
J Mol Biol. 2005 Jan 21;345(3):599-610
Authors: Shu Q, Frieden C
Adenosine deaminase (ADA, EC 3.5.4.4) is a ubiquitous (beta/alpha)8-barrel enzyme crucial for purine metabolism and normal immune competence. In this study, it was observed that loss of enzyme activity of murine ADA (mADA) precedes the global secondary and...
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11-24-2010 11:14 PM
Solution structural investigation and conformation-activity relationship of BAM8-22 b
Solution structural investigation and conformation-activity relationship of BAM8-22 by NMR and molecular dynamics simulations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Solution structural investigation and conformation-activity relationship of BAM8-22 by NMR and molecular dynamics simulations.
Bioorg Med Chem Lett. 2010 Feb 1;20(3):1260-2
Authors: Lv G, Dong S
NMR spectroscopy and molecular dynamics simulations show that BAM8-22...
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09-22-2010 05:27 AM
[NMR paper] Enzyme IIIlac of the staphylococcal phosphoenolpyruvate-dependent phosphotransferase
Enzyme IIIlac of the staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: site-specific mutagenesis of histidine residues, biochemical characterization and 1H-NMR studies.
Related Articles Enzyme IIIlac of the staphylococcal phosphoenolpyruvate-dependent phosphotransferase system: site-specific mutagenesis of histidine residues, biochemical characterization and 1H-NMR studies.
Protein Eng. 1991 Apr;4(4):469-73
Authors: Finkeldei U, Kalbitzer HR, Eisermann R, Stewart GC, Hengstenberg W
The lactose-specific phosphocarrier...
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08-21-2010 11:16 PM
[NMR paper] pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thi
pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thiobacillus yersutus as studied by 300- and 600- MHz 1H NMR.
Related Articles pH-dependent redox activity and fluxionality of the copper site in amicyanin from Thiobacillus yersutus as studied by 300- and 600- MHz 1H NMR.
J Biol Chem. 1990 Feb 15;265(5):2768-74
Authors: Lommen A, Canters GW
The kinetics of the deuteronation of one of the copper ligand histidines of the reduced Type I blue-copper protein amicyanin from Thiobacillus versutus was studied as a...
Structural and Biochemical Characterizations of Methanoredoxinfrom Methanosarcina acetivorans, aGlutaredoxin-Like Enzyme with Coenzyme M-Dependent ProteinDisulfide Reductase Activity
Linear Mode
