Bacillus subtilis deletion strains studied by 23Na NMR reveal that the antiporter-subunit MrpA and the complex I subunit NuoL are Na+-transporter proteins
Bacillus subtilis deletion strains studied by 23Na NMR reveal that the antiporter-subunit MrpA and the complex I subunit NuoL are Na+-transporter proteins
[NMR paper] NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
Related Articles NMR assignment of new thioredoxin-like protein YkuV from Bacillus subtilis.
J Biomol NMR. 2005 Jul;32(3):258
Authors: Zhang X, Yu C, Xia B, Jin C
[NMR paper] NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase
NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.
Related Articles NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.
Proc Natl Acad Sci U S A. 2003 May 13;100(10):5688-93
Authors: Nguyen BD, Abbott KL, Potempa K, Kobor MS, Archambault J, Greenblatt J, Legault P, Omichinski JG
FCP1 is the only identified phosphatase specific for the phosphorylated CTD of RNA polymerase II (RNAP II)....
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[NMR paper] Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectrosc
Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy.
Related Articles Crystallization of the Bacillus subtilis RTP-DNA complex prepared using NMR spectroscopy.
Acta Crystallogr D Biol Crystallogr. 2001 Mar;57(Pt 3):421-4
Authors: Vivian JP, Wilce JA, Hastings AF, Wilce MC
The replication terminator protein (RTP)-DNA complex of Bacillus subtilis is responsible for the arrest of DNA replication at terminator sites in the B. subtilis chromosome. The crystallization and preliminary diffraction data analysis...
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[NMR paper] Subunit-specific backbone NMR assignments of a 64 kDa trp repressor/DNA complex: a ro
Subunit-specific backbone NMR assignments of a 64 kDa trp repressor/DNA complex: a role for N-terminal residues in tandem binding.
Related Articles Subunit-specific backbone NMR assignments of a 64 kDa trp repressor/DNA complex: a role for N-terminal residues in tandem binding.
J Biomol NMR. 1998 Apr;11(3):307-18
Authors: Shan X, Gardner KH, Muhandiram DR, Kay LE, Arrowsmith CH
Deuterium decoupled, triple resonance NMR spectroscopy was used to analyze complexes of 2H, 15N, 13C labelled intact and (des2-7) trp repressor (delta 2-7 trpR) from E....
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Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Related Articles Probing the Folding Intermediate of Bacillus subtilis RNase P protein by NMR.
Biochemistry. 2010 Sep 15;
Authors: Chang YC, Franch WR, Oas TG
Protein folding intermediates are often imperative to overall folding processes and consequent biological functions. However, the low population and transient nature of the intermediate states often hinder the biochemical and biophysical characterization. Previous studies have demonstrated that Bacillus...
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[NMR paper] A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by sel
A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by selective 2H-labeling. Complete assignment and structural analysis of the aromatic resonances for a 22-kDa homodimer.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles A 1H-NMR study of the transcription factor 1 from Bacillus subtilis phage SPO1 by selective 2H-labeling. Complete assignment and structural analysis of the aromatic resonances for a 22-kDa homodimer.
Eur J...
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[NMR paper] Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-di
Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Solution structure of the phosphocarrier protein HPr from Bacillus subtilis by two-dimensional NMR spectroscopy.
Protein Sci. 1992 Oct;1(10):1363-76
Authors: Wittekind...
Bacillus subtilis deletion strains studied by 23Na NMR reveal that the antiporter-subunit MrpA and the complex I subunit NuoL are Na+-transporter proteins
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