Structural analysis of the exopolysaccharide produced by Streptococcus thermophilus S
Abstract The use of lactic acid bacteria in fermentation of milk results in favorable physical and rheological properties due to in situ exopolysaccharide (EPS) production. The EPS from S. thermophilus ST1 produces highly viscous aqueous solutions and its structure has been investigated by NMR spectroscopy. Notably, all aspects of the elucidation of its primary structure including component analysis and absolute configuration of the constituent monosaccharides were carried out by NMR spectroscopy. An array of techniques was utilized including, inter alia, PANSY and NOESY-HSQC TILT experiments. The EPS is composed of hexasaccharide repeating units with the following structure: â?? 3)[α-d-Glcp-(1 â?? 4)]-β-d-Galp-(1 â?? 4)-β-d-Glcp-(1 â?? 4)[β-d-Galf-(1 â?? 6)]-β-d-Glcp-(1 â?? 6)-β-d-Glcp-(1 â??, in which the residues in square brackets are terminal groups substituting backbone sugar residues that consequently are branch-points in the repeating unit of the polymer. Thus, the EPS consists of a backbone of four sugar residues with two terminal sugar residues making up two side-chains of the repeating unit. The molecular mass of the polymer was determined using translational diffusion experiments which resulted in Mw = 62 kDa, corresponding to 64 repeating units in the EPS.
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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11-25-2010 08:21 PM
[NMR paper] NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c
NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
Related Articles NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure.
J Biol Chem. 2004 Apr 9;279(15):15177-82
Authors: Wain R, Redfield C, Ferguson SJ, Smith LJ
Conversion of Hydrogenobacter thermophilus cytochrome c(552) into a b-type cytochrome by mutagenesis of both heme-binding cysteines to alanines significantly reduces the stability of the protein...
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11-24-2010 09:25 PM
[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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11-24-2010 09:01 PM
[NMR paper] Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in
Preliminary NMR studies of Thermus thermophilus ribosomal protein S19 overproduced in Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Preliminary 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,...
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08-22-2010 05:08 PM
[NMR paper] Optical, EPR, and 1H NMR spectroscopy of serine-ligated [2Fe-2S] ferredoxins produced
Optical, EPR, and 1H NMR spectroscopy of serine-ligated ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin.
Related Articles Optical, EPR, and 1H NMR spectroscopy of serine-ligated ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin.
Biochemistry. 1994 Mar 22;33(11):3155-64
Authors: Cheng H, Xia B, Reed GH, Markley JL
Anabaena 7120 vegetative ferredoxin is a plant-type ferredoxin that contains only...
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[NMR paper] Optical, EPR, and 1H NMR spectroscopy of serine-ligated [2Fe-2S] ferredoxins produced
Optical, EPR, and 1H NMR spectroscopy of serine-ligated ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin.
Related Articles Optical, EPR, and 1H NMR spectroscopy of serine-ligated ferredoxins produced by site-directed mutagenesis of cysteine residues in recombinant Anabaena 7120 vegetative ferredoxin.
Biochemistry. 1994 Mar 22;33(11):3155-64
Authors: Cheng H, Xia B, Reed GH, Markley JL
Anabaena 7120 vegetative ferredoxin is a plant-type ferredoxin that contains only...
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08-22-2010 03:33 AM
Enhanced production and isotope enrichment of recombinant glycoproteins produced in c
Abstract NMR studies of post-translationally modified proteins are complicated by the lack of an efficient method to produce isotope enriched recombinant proteins in cultured mammalian cells. We show that reducing the glucose concentration and substituting glutamate for glutamine in serum-free medium increased cell viability while simultaneously increasing recombinant protein yield and the enrichment of non-essential amino acids compared to culture in unmodified, serum-free medium. Adding dichloroacetate, a pyruvate dehydrogenase kinase inhibitor, further improves cell viability, recombinant...