title: ¹H, ¹³C and ¹⁵N resonance assignments of human muscle acylphosphatase.
abstract: Human muscle acylphosphatase (mAcP) is an enzyme with a ferrodoxin-like topology whose primary role is to hydrolyze the carboxyl-phosphate bonds of acylphosphates. The protein has been widely used as a model system for elucidating the molecular determinants of protein folding and misfolding. We present here the full NMR assignments of the backbone and side chains resonances of mAcP complexed with phosphate, thus providing an important resource for future solution-state NMR spectroscopic studies of the structure and dynamics of this protein in the contexts of protein folding and misfolding.
authors.affiliation: Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB21EW, UK.
authors.forename: Giuliana
authors.initials: G
authors.lastname: Fusco
authors.forename: Alfonso
authors.initials: A
authors.lastname: De Simone
authors.forename: Shang-Te Danny
authors.initials: ST
authors.lastname: Hsu
authors.forename: Francesco
authors.initials: F
authors.lastname: Bemporad
authors.forename: Michele
authors.initials: M
authors.lastname: Vendruscolo
authors.forename: Fabrizio
authors.initials: F
authors.lastname: Chiti
authors.forename: Christopher M
authors.initials: CM
authors.lastname: Dobson
mesh_terms: D017766:Acid Anhydride Hydrolases / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D009132:Muscles / Q000201:enzymology*; D019906:Nuclear Magnetic Resonance, Biomolecular; D010710:Phosphates / Q000378:metabolism; D000097024:Acylphosphatase
chemical_list: D017766:Acid Anhydride Hydrolases; D010710:Phosphates; D000097024:Acylphosphatase