Domain Motions of Inorganic pyrophosphatase from the hyperthermophile Thermococcus thioreducens Studied by NSE
The aim of this proposal is to use neutron spin-echo spectroscopy (NSE) to measure the inter-domain motions of the inorganic pyrophosphatase (IPPase) enzyme from thermostable microorganisms. IPPase derived from thermostable microorganisms is of extreme interest for biophysical studies because of their inherent chemical and thermal stability and high temperature activity. It has a hexameric quaternary structure with a molecular mass of approximately 120kDa (each subunit is about 20kDa molecular weight), which is a large oligomeric molecular structure and is supposed to have significant slow inter-domain motions. Study of this slow inter-domain motion is the key to understand why IPPase can perform catalytic activity at much higher temperature than normal enzymes, thus enables bacteria to survive under extremely high temperature.
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SHARP Melissa; Xiang-qiang Chu; COATES Leighton; CZAKKEL Orsolya and NG Joseph. (2015). Domain Motions of Inorganic pyrophosphatase from the hyperthermophile Thermococcus thioreducens Studied by NSE. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-689
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