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1H, 13C and 15N chemical shift assignments of unliganded Bcl-xL and its complex with a photoresponsive Bak-derived peptide |
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| Authors: | Piotr Wysoczanski Robert J. Mart E. Joel Loveridge Christopher Williams Sara B.-M. Whittaker Matthew P. Crump Rudolf K. Allemann |
| Affiliation: | 1. School of Chemistry, Cardiff University, Park Place, Cardiff, CF10 3AT, UK 4. Institute of Life Sciences, Swansea University, Singleton Park, Swansea, SA2 8PP, UK 2. School of Chemistry, University of Bristol, Cantock’s Close, Bristol, BS8 1TS, UK 3. School of Cancer Studies, University of Birmingham, Vincent Drive, Birmingham, B15 2TT, UK |
| Abstract: | Here we report the 1H, 13C and 15N resonance assignments of free Bcl-xL and of Bcl-xL 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. |
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