ARTICLE 1 H, 13 C and 15 N resonance assignments of human muscle acylphosphatase Giuliana Fusco • Alfonso De Simone • Shang-Te Danny Hsu • Francesco Bemporad • Michele Vendruscolo • Fabrizio Chiti • Christopher M. Dobson Received: 5 March 2011 / Accepted: 23 May 2011 / Published online: 5 June 2011 Ó Springer Science+Business Media B.V. 2011 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 reso- nances 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. Keywords Human muscle acylphosphatase Á Ferrodoxin-like fold Á Hydrolase Á Protein folding and misfolding Biological context Human muscle acylphosphatase (mAcP) is a small (*11 kDa) enzyme that specifically catalyzes the hydro- lysis of the carboxyl-phosphate bond of acylphosphates (Stefani et al. 1997). mAcP has a ferredoxin-like topology, consisting of five b-strands (S1–S5) arranged in a single b-sheet and two a-helices (H1 and H2), and is produced in a wide variety of species and tissues. In the past two dec- ades mAcP has attracted the interest of the biophysical community because of its functional relevance and also for the large number of studies on this protein that have con- tributed significantly to our understanding of the principles of protein folding (Chiti et al. 1999) and misfolding (Chiti et al. 2000, 2003). Indeed mAcP has proved to be an appropriate system to probe the generic mechanisms that result in normally soluble and stable proteins aggregating into insoluble thread-like amyloid fibrils (Chiti et al. 2000, 2003). These processes are of very considerable impor- tance as they are linked to a group of fatal neurodegener- ative disorders, including Alzheimer’s and Parkinson’s disease, as well as non-neuropathic diseases, including systemic amyloidoses and type II diabetes (Chiti and Dobson 2006). Despite this interest in folding and mis- folding of mAcP, assignments of its NMR resonances have not previously been reported. The present work therefore opens to high-resolution NMR investigations designed to reveal the atomic details of the various steps in the protein folding and misfolding processes of mAcP that have been identified for this system by other biophysical techniques. The mAcP native structure analysed here is complexed with phosphate. Methods and experiments Sample preparation Purification of mAcP was performed as described previ- ously (Modesti et al. 1993). 1 H, 15 N, 13 C labelled protein G. Fusco Á A. De Simone Á F. Bemporad Á M. Vendruscolo Á C. M. Dobson (&) Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB21EW, UK e-mail: cmd44@cam.ac.uk S.-T. D. Hsu Institute of Bioinformatics and Structural Biology, National Tsing Hua University, 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan F. Chiti Department of Biochemical Sciences, University of Florence, Viale Morgagni 50, 50134 Florence, Italy 123 Biomol NMR Assign (2012) 6:27–29 DOI 10.1007/s12104-011-9318-1