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@article{1403068,
author = {Mazurenko, Stanislav and Kunka, Antonín and Beerens, Koen and Johnson, Christopher M. and Damborský, Jiří and Prokop, Zbyněk},
article_location = {London},
article_number = {November},
doi = {http://dx.doi.org/10.1038/s41598-017-16360-y},
keywords = {DIFFERENTIAL SCANNING CALORIMETRY; THERMAL-DENATURATION; THEORETICAL-ANALYSIS; AGGREGATION; STABILITY; LYSOZYME; STABILIZATION; SPECTROSCOPY; TRANSITIONS; PROFILES},
language = {eng},
issn = {2045-2322},
journal = {Scientific Reports},
title = {Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating},
url = {https://loschmidt.chemi.muni.cz/peg/publications/exploration-of-protein-unfolding-by-modelling-calorimetry-data-from-reheating/},
volume = {7},
year = {2017}
}
TY - JOUR
ID - 1403068
AU - Mazurenko, Stanislav - Kunka, Antonín - Beerens, Koen - Johnson, Christopher M. - Damborský, Jiří - Prokop, Zbyněk
PY - 2017
TI - Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating
JF - Scientific Reports
VL - 7
IS - November
SP - nestránkováno
EP - nestránkováno
PB - NATURE PUBLISHING GROUP
SN - 20452322
KW - DIFFERENTIAL SCANNING CALORIMETRY
KW - THERMAL-DENATURATION
KW - THEORETICAL-ANALYSIS
KW - AGGREGATION
KW - STABILITY
KW - LYSOZYME
KW - STABILIZATION
KW - SPECTROSCOPY
KW - TRANSITIONS
KW - PROFILES
UR - https://loschmidt.chemi.muni.cz/peg/publications/exploration-of-protein-unfolding-by-modelling-calorimetry-data-from-reheating/
N2 - 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, (iii) partially reversible transitions, and (iv) general three-state models. The method is validated using calorimetry data for chicken egg lysozyme, mutated Protein A, three wild-types of haloalkane dehalogenases, and a mutant stabilized by protein engineering. We show that modelling of reheating increases the precision of determination of unfolding mechanisms, free energies, temperatures, and heat capacity differences. Moreover, this modelling indicates whether alternative refolding pathways might occur upon cooling. The Matlab-based data fitting software tool and its user guide are provided as a supplement.
ER -
MAZURENKO, Stanislav, Antonín KUNKA, Koen BEERENS, Christopher M. JOHNSON, Jiří DAMBORSKÝ a Zbyněk PROKOP. Exploration of Protein Unfolding by Modelling Calorimetry Data from Reheating. \textit{Scientific Reports}. London: NATURE PUBLISHING GROUP, roč.~7, November, s.~nestránkováno, 14 s. ISSN~2045-2322. doi:10.1038/s41598-017-16360-y. 2017.
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