Title |
1H, 13C and 15N chemical shift assignments of unliganded Bcl-xL and its complex with a photoresponsive Bak-derived peptide
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Published in |
Biomolecular NMR Assignments, June 2012
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DOI | 10.1007/s12104-012-9407-9 |
Pubmed ID | |
Authors |
Piotr Wysoczanski, Robert J. Mart, E. Joel Loveridge, Christopher Williams, Sara B.-M. Whittaker, Matthew P. Crump, Rudolf K. Allemann |
Abstract |
Here we report the (1)H, (13)C and (15)N resonance assignments of free Bcl-x(L) and of Bcl-x(L) in complex with an azobenzene-modified peptide derived from the BH3 domain of the pro-apoptotic Bak. The spectra suggest predominantly folded proteins; chemical shift difference analysis provides a detailed view of the reorganization occurring on peptide binding. |
Mendeley readers
The data shown below were compiled from readership statistics for 13 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
Country | Count | As % |
---|---|---|
Unknown | 13 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
---|---|---|
Student > Ph. D. Student | 4 | 31% |
Student > Master | 3 | 23% |
Researcher | 2 | 15% |
Lecturer | 1 | 8% |
Student > Bachelor | 1 | 8% |
Other | 0 | 0% |
Unknown | 2 | 15% |
Readers by discipline | Count | As % |
---|---|---|
Chemistry | 5 | 38% |
Agricultural and Biological Sciences | 3 | 23% |
Pharmacology, Toxicology and Pharmaceutical Science | 1 | 8% |
Medicine and Dentistry | 1 | 8% |
Environmental Science | 1 | 8% |
Other | 0 | 0% |
Unknown | 2 | 15% |