1H, 13C and 15N chemical shift assignments of unliganded Bcl-xL and its complex with a photoresponsive Bak-derived peptide

Wysoczanski, Piotr, Mart, Robert J. ORCID: https://orcid.org/0000-0003-2196-5840, Loveridge, Edric Joel, Williams, Christopher, Whittaker, Sara B.-M., Crump, Matthew P. and Allemann, Rudolf Konrad ORCID: https://orcid.org/0000-0002-1323-8830 2013. 1H, 13C and 15N chemical shift assignments of unliganded Bcl-xL and its complex with a photoresponsive Bak-derived peptide. Biomolecular NMR Assignments 7 (2) , pp. 187-191. 10.1007/s12104-012-9407-9

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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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Chemistry Research Institutes & Centres > Cardiff Catalysis Institute (CCI)
Subjects:	Q Science > QD Chemistry
Uncontrolled Keywords:	Bcl-xL – Bcl-2 family – Photonano-switches – Azobenzene
Publisher:	Springer
ISSN:	1874-2718
Funders:	EPSRC, Wellcome Trust
Last Modified:	21 Oct 2022 09:38
URI:	https://orca.cardiff.ac.uk/id/eprint/37169

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