¹H, ¹³C, and ¹⁵N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis.
Publication
, Journal Article
Olson, AL; Bobay, BG; Melander, C; Cavanagh, J
Published in: Biomolecular NMR assignments
April 2012
The AbrB protein is a transcription factor that regulates the expression of numerous essential genes during the cells transition phase state. AbrB from Bacillus anthracis is, nototriously, the principal protein responsible for anthrax toxin gene expression and is highly homologous to the much-studied AbrB protein from Bacillus subtilis having 85% sequence identity and the ability to regulate the same target promoters. Here we report backbone and sidechain resonance assignments and secondary structure prediction for the full-length AbrB protein from B. anthracis.
Duke Scholars
Published In
Biomolecular NMR assignments
DOI
EISSN
1874-270X
ISSN
1874-2718
Publication Date
April 2012
Volume
6
Issue
1
Start / End Page
95 / 98
Related Subject Headings
- Transcription Factors
- Protein Structure, Secondary
- Nuclear Magnetic Resonance, Biomolecular
- DNA-Binding Proteins
- Biophysics
- Bacterial Proteins
- Bacillus anthracis
- 3101 Biochemistry and cell biology
- 0601 Biochemistry and Cell Biology
Citation
APA
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ICMJE
MLA
NLM
Olson, A. L., Bobay, B. G., Melander, C., & Cavanagh, J. (2012). ¹H, ¹³C, and ¹⁵N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis. Biomolecular NMR Assignments, 6(1), 95–98. https://doi.org/10.1007/s12104-011-9333-2
Olson, Andrew L., Benjamin G. Bobay, Christian Melander, and John Cavanagh. “¹H, ¹³C, and ¹⁵N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis.” Biomolecular NMR Assignments 6, no. 1 (April 2012): 95–98. https://doi.org/10.1007/s12104-011-9333-2.
Olson AL, Bobay BG, Melander C, Cavanagh J. ¹H, ¹³C, and ¹⁵N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis. Biomolecular NMR assignments. 2012 Apr;6(1):95–8.
Olson, Andrew L., et al. “¹H, ¹³C, and ¹⁵N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis.” Biomolecular NMR Assignments, vol. 6, no. 1, Apr. 2012, pp. 95–98. Epmc, doi:10.1007/s12104-011-9333-2.
Olson AL, Bobay BG, Melander C, Cavanagh J. ¹H, ¹³C, and ¹⁵N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis. Biomolecular NMR assignments. 2012 Apr;6(1):95–98.
Published In
Biomolecular NMR assignments
DOI
EISSN
1874-270X
ISSN
1874-2718
Publication Date
April 2012
Volume
6
Issue
1
Start / End Page
95 / 98
Related Subject Headings
- Transcription Factors
- Protein Structure, Secondary
- Nuclear Magnetic Resonance, Biomolecular
- DNA-Binding Proteins
- Biophysics
- Bacterial Proteins
- Bacillus anthracis
- 3101 Biochemistry and cell biology
- 0601 Biochemistry and Cell Biology