Related ArticlesPreliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli.
FEBS Lett. 1997 Sep 29;415(2):155-9
Authors: Davydova NL, Rak AV, Gryaznova OI, Liljas A, Jonsson BH, Berglund H, Härd T, Garber MB
The gene for the ribosomal protein S19 from Thermus thermophilus was cloned, sequenced and overexpressed in Escherichia coli. A simple procedure for isolating the recombinant protein was developed. Preliminary NMR studies revealed a high content of alpha-helical secondary structure in the protein.
Active site dynamics in NADH oxidase from Thermus thermophilus studied by NMR spin relaxation
Active site dynamics in NADH oxidase from Thermus thermophilus studied by NMR spin relaxation
Abstract We have characterized the backbone dynamics of NADH oxidase from Thermus thermophilus (NOX) using a recently-developed suite of NMR experiments designed to isolate exchange broadening, together with 15N R 1, R 1Ï? , and {1H}-15N steady-state NOE relaxation measurements performed at 11.7 and 18.8 T. NOX is a 54 kDa homodimeric enzyme that belongs to a family of structurally homologous flavin reductases and nitroreductases with many potential biotechnology applications. Prior studies...
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[NMR paper] NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70
NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone.
Related Articles NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone.
J Mol Biol. 2005 May 27;349(1):163-83
Authors: Revington M, Zhang Y, Yip GN, Kurochkin AV, Zuiderweg ER
Hsp70 chaperones are two-domain proteins that assist in intra-cellular protein (re) folding processes in all species. The protein folding activity of the substrate binding domain of the Hsp70s is regulated by...
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[NMR paper] NMR structure of the ribosomal protein L23 from Thermus thermophilus.
NMR structure of the ribosomal protein L23 from Thermus thermophilus.
Related Articles NMR structure of the ribosomal protein L23 from Thermus thermophilus.
J Biomol NMR. 2003 Jun;26(2):131-7
Authors: Ohman A, Rak A, Dontsova M, Garber MB, Härd T
The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus. Uncomplexed L23...
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[NMR paper] Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the e
Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III.
Related Articles Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the epsilon subunit of Escherichia coli DNA polymerase III.
J Struct Biol. 2000 Aug;131(2):164-9
Authors: Hamdan S, Brown SE, Thompson PR, Yang JY, Carr PD, Ollis DL, Otting G, Dixon NE
The structured core of the N-terminal 3'-5' exonuclease domain of epsilon, the proofreading subunit of Escherichia coli DNA...
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NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermo
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
Related Articles NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
J Struct Funct Genomics. 2010 Oct 5;
Authors: Goroncy AK, Murayama K, Shirouzu M, Kuramitsu S, Kigawa T, Yokoyama S
Sterol carrier protein 2 (SCP-2), also known as nonspecific lipid transfer protein, is a ubiquitous intracellular ~13*kDa protein found in mammals, insects, plants,...
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[NMR paper] Ribosomal protein S17: characterization of the three-dimensional structure by 1H and
Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Related Articles Ribosomal protein S17: characterization of the three-dimensional structure by 1H and 15N NMR.
Biochemistry. 1993 Nov 30;32(47):12812-20
Authors: Golden BL, Hoffman DW, Ramakrishnan V, White SW
The structure of ribosomal protein S17 from Bacillus stearothermophilus was investigated by two-dimensional homonuclear and heteronuclear magnetic resonance spectroscopy. The 1H and 15N chemical shift assignments are largely complete, and a...
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[NMR paper] Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
Related Articles Purification of cloned trypanosomal calmodulin and preliminary NMR studies.
J Chromatogr. 1991 Feb 22;539(2):501-5
Authors: Sweeney PJ, Walker JM, Reid DG, Elshourbagy N
Cloned trypanosomal calmodulin was expressed in Escherichia coli and purified to homogeneity using hydrophobic interaction chromatography on phenyl-Sepharose. The purified protein was subjected to NMR analysis which allows detailed changes to be observed when, firstly, calcium, and...
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[NMR paper] 1H NMR studies on bovine cyclophilin: preliminary structural characterization of its
1H NMR studies on bovine cyclophilin: preliminary structural characterization of its complex with cyclosporin A.
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Biochemistry. 1990 May 8;29(18):4466-78
Authors: Heald SL, Harding MW, Handschumacher RE, Armitage IM
Cyclophilin (163 residues, Mr 17737), a peptidyl prolyl cis-trans isomerase, is a cytosolic protein that specifically binds the potent immunosuppressant cyclosporin A (CsA). The native form of the major...
Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in
Linear Mode
