CalFitter: a web server for analysis of protein thermal denaturation data

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Publikace nespadá pod Filozofickou fakultu, ale pod Přírodovědeckou fakultu. Oficiální stránka publikace je na webu muni.cz.
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MAZURENKO Stanislav ŠTOURAČ Jan KUNKA Antonín NEDELJKOVIC S. BEDNÁŘ David PROKOP Zbyněk DAMBORSKÝ Jiří

Rok publikování 2018
Druh Článek v odborném periodiku
Časopis / Zdroj Nucleic Acids Research
Fakulta / Pracoviště MU

Přírodovědecká fakulta

Citace
www https://loschmidt.chemi.muni.cz/peg/category/publications/#2018
Doi http://dx.doi.org/10.1093/nar/gky358
Klíčová slova DIFFERENTIAL SCANNING CALORIMETRY; THEORETICAL-ANALYSIS; STABILITY; STATE; TEMPERATURE; 3-STATE; ENZYME; RATES
Popis Despite significant advances in the understanding of protein structure-function relationships, revealing protein folding pathways still poses a challenge due to a limited number of relevant experimental tools. Widely-used experimental techniques, such as calorimetry or spectroscopy, critically depend on a proper data analysis. Currently, there are only separate data analysis tools available for each type of experiment with a limited model selection. To address this problem, we have developed the CalFitter web server to be a unified platform for comprehensive data fitting and analysis of protein thermal denaturation data. The server allows simultaneous global data fitting using any combination of input data types and offers 12 protein unfolding pathway models for selection, including irreversible transitions often missing from other tools. The data fitting produces optimal parameter values, their confidence intervals, and statistical information to define unfolding pathways. The server provides an interactive and easy-to-use interface that allows users to directly analyse input datasets and simulate modelled output based on the model parameters.
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