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

Author

Wysoczanski P, Mart RJ, Loveridge EJ, Williams C, Whittaker SB, Crump MP, and Allemann RK

Subjects
Amino Acid Sequence, Carbon Isotopes, Ligands, Nitrogen Isotopes, Peptides chemistry, bcl-2 Homologous Antagonist-Killer Protein metabolism, Light, Nuclear Magnetic Resonance, Biomolecular, Peptides metabolism, Protons, bcl-2 Homologous Antagonist-Killer Protein chemistry, bcl-X Protein chemistry, bcl-X Protein metabolism
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.

Published
2013
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