The relation of protein folding and dynamics investigated with wide-angle NSE
We suggest to investigate the correlation between protein folding and dynamics for apomyoglobin in native folded conformations, partially folded intermediates and denatured states. We propose to use wide-angle neutron spin-echo spectroscopy (NSE) on WASP to measure average protein dynamics in the incoherent scattering range. The experiment on WASP would allow us to access a time range from the ps to several ns. This broad time window would enable us to measure both global diffusion and internal protein dynamics. Our guess is that in the fully unfolded state at high concentration of the denaturant guanidinium hydrochloride internal protein dynamics should show a pure polymer-like behavior, whereas as the secondary structure content is increased more complex dynamics will emerge for the partially folded intermediates. Finally, the fully folded Mb would be most-likely more rigid as the secondary structure elements are permanently folded. The experiment on WASP would allow us to identify fast motional patters that sit on top of slow collective motions that were identified recently by NSE experiments using coherent neutron scattering (Balacescu et al. Scientific Reports 2020, 10:1570).
Please note that you will need to login with your ILL credentials to download the data.
Download DataThe recommended format for citing this dataset in a research publication is in the following format:
Andreas M. Stadler; FALUS Peter; HARIS Luman and Tobias E. Schrader. (2021). The relation of protein folding and dynamics investigated with wide-angle NSE. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-04-903
ILL has partnered with DataCite as the registration agency
for data persistent identifiers.