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. © 2011 Springer Science+Business Media B.V.
1H, 13C and 15N resonance assignments of human muscle acylphosphatase / Fusco, G.; De Simone, A.; Hsu, S. -T. D.; Bemporad, F.; Vendruscolo, M.; Chiti, F.; Dobson, C. M.. - In: BIOMOLECULAR NMR ASSIGNMENTS. - ISSN 1874-2718. - 6:1(2012), pp. 27-29. [10.1007/s12104-011-9318-1]
1H, 13C and 15N resonance assignments of human muscle acylphosphatase
Fusco G.;De Simone A.;
2012
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. © 2011 Springer Science+Business Media B.V.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
