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

Biomol NMR Assign. 2013 Oct;7(2):187-91. doi: 10.1007/s12104-012-9407-9. Epub 2012 Jun 30.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

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

Substances

  • Carbon Isotopes
  • Ligands
  • Nitrogen Isotopes
  • Peptides
  • Protons
  • bcl-2 Homologous Antagonist-Killer Protein
  • bcl-X Protein