Journal
BIOMOLECULAR NMR ASSIGNMENTS
Volume 6, Issue 1, Pages 27-29Publisher
SPRINGER
DOI: 10.1007/s12104-011-9318-1
Keywords
Human muscle acylphosphatase; Ferrodoxin-like fold; Hydrolase; Protein folding and misfolding
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Funding
- MRC
- EPSRC
- Marie Curie
- HSFP
- Italian Ministero dell'Istruzione dell'Universita e della Ricerca
- National Science Council of the Republic of China-Taiwan
- BBSRC
- Royal Society
- BBSRC [BB/H003843/1] Funding Source: UKRI
- EPSRC [EP/G049998/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/H003843/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/G049998/1] Funding Source: researchfish
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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.
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