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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Carbon Isotopes
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Ligands
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Light*
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Nitrogen Isotopes
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Nuclear Magnetic Resonance, Biomolecular*
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Peptides / chemistry
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Peptides / metabolism*
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Protons*
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bcl-2 Homologous Antagonist-Killer Protein / chemistry*
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bcl-2 Homologous Antagonist-Killer Protein / metabolism
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bcl-X Protein / chemistry*
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bcl-X Protein / metabolism*
Substances
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Carbon Isotopes
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Ligands
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Nitrogen Isotopes
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Peptides
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Protons
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bcl-2 Homologous Antagonist-Killer Protein
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bcl-X Protein