Abstract
Protein dynamics or protein motions are believed to ultimately govern the biological function and activities of protein. Quasielastic neutron scattering (QENS) technique has been proven to be an exceptional tool to study dynamics of proteins in the time scale of picosecond (ps) to nanosecond (ns) [1, 2]. In this study, we use QENS to investigate how a large oligomeric protein, Inorganic Pyrophosphatase (IPPase) from Thermococcus thioreducens with quaternary structural complexity, have distinguishable dynamic characteristics compared to those of the small simple monomeric model protein, lysozyme.
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