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Persistent URL http://purl.org/net/epubs/work/65698
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Record Id 65698
Title Mean squared displacement analysis of an-harmonic behaviour in lyophilised proteins
Abstract The temperature dependence of the mean squared displacement (msd), r(T)2, determined from three lyophilised proteins (apoferritin, green fluorescent protein and insulin) observed over two different experimental time scales is presented. The r2 parameter at each temperature is computed via analysis of elastic incoherent neutron scattering data. Fast pico-second (ps) dynamics appear insensitive to the secondary structure of the proteins. However, the arrangement of the amino acids appears to play a role at longer nano-second (ns) timescales. The effect of hydration on r(T)2 is also considered. For apoferritin and green fluorescent protein, elevated hydration levels appear to suppress fast ps dynamic modes when T < 240 K rendering the material more rigid than when in its lyophilised state.
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Language English (EN)
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Journal Article Chem Phys 424 (2013): 32-36. doi:10.1016/j.chemphys.2013.05.008 2013