The contribution of thermal fluctuations to protein folding
Folding of a protein into its functional structure can be described in thermodynamic terms by the difference in Gibb’s free energy dG between the unfolded and the folded state dG=dH-T*dS. Protein conformational fluctuations and disordered water molecules in the hydration shell account for the entropic contribution T*dS. The aim of this neutron scattering study is to quantify the contribution of protein conformational fluctuations to entropic stability of different folded states of apomyoglobin by quasielastic neutron scattering in the ps and ns time scale. The proposal covers two aspects: i) The continuation on IN6 would allow us to complete our first IN6 experiment by measuring the fully unfolded state, and characterize another folding intermediate with 28% structure and finally the fully folded state of myoglobin with 66% secondary structure. ii) The IN16 neutron spectrometer would allow us to investigate the role of conformational fluctuations in a different time windows of several ns. By combining the IN6 and IN16 results we could deduce if fluctuations in the ps or the ns time scale are the driving force for conformational stabilization in protein folding.
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Andreas M. Stadler; Bernhard Frick; KOZA Michael Marek; RICHTER Dieter and SEYDEL Tilo. (2013). The contribution of thermal fluctuations to protein folding. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-688
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