Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating.

ABSTRACT: Studies of protein unfolding mechanisms are critical for understanding protein functions inside cells, de novo protein design as well as defining the role of protein misfolding in neurodegenerative disorders. Calorimetry has proven indispensable in this regard for recording full energetic profiles of protein unfolding and permitting data fitting based on unfolding pathway models. While both kinetic and thermodynamic protein stability are analysed by varying scan rates and reheating, the latter is rarely used in curve-fitting, leading to a significant loss of information from experiments. To extract this information, we propose fitting both first and second scans simultaneously. Four most common single-peak transition models are considered: (i) fully reversible, (ii) fully irreversible, (ii

SUBMITTER: Mazurenko S 

PROVIDER: S-EPMC5701188 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature