The correlation between protein folding and dynamics investigated using high-resolution neutron TOF spectroscopy.
The aim of the proposal is the investigation of the underlying correlation between protein dynamics and protein folding in apomyoglobin (apoMb). We will measure three samples of apoMb: the unfolded state of apoMb at pH2, one folding intermediate stabilized by NaCl with 28% helical content as an example of a folding intermediate and the fully folded state of apoMb (55% helical content). From high-resolution QENS measurements on IN5 of protein solutions we can separate internal dynamics and global diffusion. Good statistics of the quasielastic signal will allow us to interpret the internal dynamics with analytical theories such as the model for Brownian diffusion in a harmonic potential or the model for fractional Brownian dynamics in a harmonic potential. From temperature dependent measurements we will determine the evolution of the entropic stabilisation Delta S with temperature, and gain information about forces within the unfolded, partially folded and fully folded structures, which are related to the enthalpic stabilisation Delta H.
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Andreas M. Stadler; OLLIVIER Jacques and RICHTER Dieter. (2014). The correlation between protein folding and dynamics investigated using high-resolution neutron TOF spectroscopy.. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-709
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