NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633.
NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633.
NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633.
Biomol NMR Assign. 2011 Jun 5;
Authors: Christ NA, Duchardt-Ferner E, Düsterhus S, Kötter P, Entian KD, Wöhnert J
Bacillus subtilis ATCC 6633 produces the lipid II targeting lantibiotic subtilin. For self-protection these gram-positive bacteria express a cluster of four self-immunity proteins named SpaIFEG. SpaI is a 16.8*kDa lipoprotein which is attached to the...
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[NMR paper] Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.
Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.
Related Articles Interaction of the replication terminator protein of Bacillus subtilis with DNA probed by NMR spectroscopy.
Biochem Biophys Res Commun. 2005 Sep 23;335(2):361-6
Authors: Hastings AF, Otting G, Folmer RH, Duggin IG, Wake RG, Wilce MC, Wilce JA
Termination of DNA replication in Bacillus subtilis involves the polar arrest of replication forks by a specific complex formed between the dimeric 29 kDa replication terminator...
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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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11-19-2010 08:32 PM
[NMR paper] NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible d
NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability.
Related Articles NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability.
Eur J Biochem. 2000 Jan;267(2):403-13
Authors: Nicastro G, De Chiara C, Pedone E, Tatò M, Rossi M, Bartolucci S
The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx), an eubacterium growing optimally at 333 K, is the first Trx described to date from a moderate thermophilic source. To...
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11-18-2010 09:15 PM
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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09-17-2010 04:14 PM
[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...
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[NMR paper] Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spect
Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
Related Articles Sequence-specific 1H NMR resonance assignments of Bacillus subtilis HPr: use of spectra obtained from mutants to resolve spectral overlap.
Biochemistry. 1990 Aug 7;29(31):7191-200
Authors: Wittekind M, Reizer J, Klevit RE
On the basis of an analysis of two-dimensional 1H NMR spectra, the complete sequence-specific 1H NMR assignments are presented for the phosphocarrier protein HPr from the...