The role of internal dynamics and resilience on protein unfolding investigated by means of pressure modulation
In order to get insight on the role of internal dynamics on the protein folding/unfolding transition, we propose here to study the internal motions of myoglobin in the temperature range 273-363 K, at different pressure values, from 0 to 5 kbar. Our aim is to investigate the relation between the dynamics/softness of the protein and its thermal/pressure stability. In fact, measurement of elastic scans in the temperature range 273-363 K and at various pressure values will enable us to put in relation the internal dynamics of the protein, as reflected in the Mean Square Displacements (MSD) of non-exchangeable hydrogen atoms, and its pressure-dependent unfolding temperature (as obtained from a high temperature abrupt change in the MSD behavior). The obtained results will give important information on the correlation between protein internal dynamics and unfolding and in particular on the existence of a unique dynamical regime in the proximity of the unfolding process, as recently suggested. In addition, thermodynamic quantities as free energy, enthalpy and entropy will be extracted and compared to values obtained by calorimetry and densitometry.
The data is currently only available to download if you are a member of the proposal team.
The recommended format for citing this dataset in a research publication is in the following format:
LIBRIZZI Fabio; Antonino Caliņ; CARROTTA Rita; CISSE Aline; CUPANE Antonio; ORECCHINI Andrea; PETERS Judith and ZELLER Dominik. (2020). The role of internal dynamics and resilience on protein unfolding investigated by means of pressure modulation. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.CRG-2653
This data is not yet public
This data is not yet public
ILL has partnered with DataCite as the registration agency
for data persistent identifiers.