title: ¹H, ¹³C and ¹⁵N chemical shift assignments of unliganded Bcl-xL and its complex with a photoresponsive Bak-derived peptide.
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.
authors: School of Chemistry, Cardiff University, Park Place, Cardiff CF10 3AT, UK.
authors: Piotr
authors: P
authors: Wysoczanski
authors: Robert J
authors: RJ
authors: Mart
authors: E Joel
authors: EJ
authors: Loveridge
authors: Christopher
authors: C
authors: Williams
authors: Sara B-M
authors: SB
authors: Whittaker
authors: Matthew P
authors: MP
authors: Crump
authors: Rudolf K
authors: RK
authors: Allemann
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D008024:Ligands; D008027:Light; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D011522:Protons; D050998:bcl-2 Homologous Antagonist-Killer Protein / Q000737:chemistry* / Q000378:metabolism; D051020:bcl-X Protein / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D002247:Carbon Isotopes; D008024:Ligands; D009587:Nitrogen Isotopes; D010455:Peptides; D011522:Protons; D050998:bcl-2 Homologous Antagonist-Killer Protein; D051020:bcl-X Protein