Related ArticlesComparison of the X-ray structure of native rubredoxin from Pyrococcus furiosus with the NMR structure of the zinc-substituted protein.
Protein Sci. 1992 Nov;1(11):1522-5
Authors: Blake PR, Day MW, Hsu BT, Joshua-Tor L, Park JB, Hare DR, Adams MW, Rees DC, Summers MF
The three-dimensional X-ray structures of the oxidized and reduced forms of rubredoxin from Pyrococcus furiosus, determined at -161 degrees C, and the NMR structure of the zinc-substituted protein, determined in solution at 45 degrees C, are compared. The NMR and X-ray structures, which were determined independently, are very similar and lead to similar conclusions regarding the interactions that confer hyperthermostability.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt 9):1148-53
Authors: Buchko GW, Hewitt SN, Napuli AJ, Van Voorhis WC, Myler PJ
Abstract
Owing to the evolution of multi-drug-resistant and extremely drug-resistant Mycobacterium tuberculosis strains,...
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(1)H, (13)C, and (15)N NMR assignments of the Pyrococcus abyssi DNA polymerase II intein.
(1)H, (13)C, and (15)N NMR assignments of the Pyrococcus abyssi DNA polymerase II intein.
(1)H, (13)C, and (15)N NMR assignments of the Pyrococcus abyssi DNA polymerase II intein.
Biomol NMR Assign. 2011 Apr 26;
Authors: Liu J, Du Z, Albracht CD, Naidu RO, Mills KV, Wang C
Protein splicing is a precise post-translational process mediated by inteins. Inteins are intervening proteins that cleave themselves from a precursor protein while joining the flanking sequences. Here we report the (15)N, (13)C, and (1)H chemical shift assignments of the intein...
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[NMR paper] Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by
Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase.
Related Articles Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase.
Biochemistry. 2004 Mar 23;43(11):3167-82
Authors: Perry A, Tambyrajah W, Grossmann JG, Lian LY, Scrutton NS
Here we provide insights into the molecular structure of the two-iron...
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[NMR paper] Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Related Articles Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.
Protein Sci. 2003 Dec;12(12):2823-30
Authors: Aramini JM, Huang YJ, Cort JR, Goldsmith-Fischman S, Xiao R, Shih LY, Ho CK, Liu J, Rost B, Honig B, Kennedy MA, Acton TB, Montelione GT
We report NMR assignments and solution structure of the 71-residue 30S ribosomal protein S28E from the archaean Pyrococcus horikoshii, target JR19 of the Northeast Structural...
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[NMR paper] NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabili
NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes.
Related Articles NMR structure of Desulfovibrio gigas rubredoxin: a model for studying protein stabilization by compatible solutes.
Extremophiles. 2001 Oct;5(5):303-11
Authors: Lamosa P, Brennan L, Vis H, Turner DL, Santos H
Rubredoxins are small, soluble proteins that display a wide variation in thermostability, despite having a high degree of sequence similarity They also vary in the extent to which they are stabilized by...
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11-19-2010 08:44 PM
[NMR paper] 1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus t
1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure.
Related Articles 1H NMR investigation of the paramagnetic cluster environment in Pyrococcus furiosus three-iron ferredoxin: sequence-specific assignment of ligated cysteines independent of tertiary structure.
Biochemistry. 1995 Jan 17;34(2):600-10
Authors: Gorst CM, Yeh YH, Teng Q, Calzolai L, Zhou ZH, Adams MW, La Mar GN
One- and two-dimensional 1H NMR...
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[NMR paper] Comparison of native and mutant proteins provides a sequence-specific assignment of t
Comparison of native and mutant proteins provides a sequence-specific assignment of the cysteinyl ligand proton NMR resonances in the 2 ferredoxin from Clostridium pasteurianum.
Related Articles Comparison of native and mutant proteins provides a sequence-specific assignment of the cysteinyl ligand proton NMR resonances in the 2 ferredoxin from Clostridium pasteurianum.
Biochemistry. 1994 Dec 6;33(48):14486-95
Authors: Scrofani SD, Brereton PS, Hamer AM, Lavery MJ, McDowall SG, Vincent GA, Brownlee RT, Hoogenraad NJ, Sadek M, Wedd AG
A...
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[MWClarkson blog] How native-like is a cold-denatured structure?
How native-like is a cold-denatured structure?
http://www.researchblogging.org/public/citation_icons/rb2_large_gray.pngA protein has several different levels of structure. The primary structure is the arrangements of atoms and bonds, and it is formed in the ribosome by the assembly of amino acids as directed by an RNA template. The secondary structure is the local topology, the helices and strands, and this forms mostly because of the release of energy through the formation of hydrogen bonds. The tertiary structure is the actual fold of the protein, the way helices, strands, and loops are...