Identifying the geometry of pico-second motion in lyophilised proteins
We recently used IN16 to study ps-ns dynamics in lyophilized proteins (apoferritin, green fluorescent protein, superoxide dismutase and insulin) By operating IN16 in elastic fixed window mode (EFWS) we showed that while only CH3 activation is apparent in Apo, a more enhanced dynamic environment is evident in Ins, SOD and GfP; a second, possibly structure dependent, dynamic contribution being required to describe the data The origin of this extra component is unclear Due to the limited Q range afforded by IN16 no information about the geometry of motion associated with the second component could be inferred from the elastic incoherent structure factor, EISF. Indeed, the EISF of the second process in all three proteins showed a weak Q dependence which could be modelled by either the response predicted for protons undergoing 2-site jumps or for protons diffusing on a sphere. To distinguish between these two models we now ask for time on IN13 to perform complementary EFWS measurements on Apo, SOD, Ins and GfP The greatly extended Q range on IN13 will allow us to ascertain which motion is applicable; deviation from either prediction perhaps suggesting an alternative diffusive response
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Mark T F Telling; Luke A. Clifton; GARCIA SAKAI Victoria and NATALI Francesca. (2013). Identifying the geometry of pico-second motion in lyophilised proteins. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.9-13-482
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