Novel mechanistic insights into the pressure and temperature stabilization of enzymes

Authors
Vasilchuk, Daniel
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Other Contributors
Makhatadze, George I.
Barquera, Blanca L.
Colón, Wilfredo
Dinolfo, Peter
García, Angel E.
Issue Date
2016-08
Keywords
Chemistry
Degree
PhD
Terms of Use
This electronic version is a licensed copy owned by Rensselaer Polytechnic Institute, Troy, NY. Copyright of original work retained by author.
Full Citation
Abstract
Pressure perturbation calorimetry (PPC) was used to determine the volumetric properties for a diverse set of globular proteins, including six ancestral thioredoxins (Trx). The thermal expansion coefficient in the native state as a function of temperature (αN (T)) was shown to be very different for the studied proteins. After eliminating various structural and thermodynamic factors it was concluded that the differences in the native state expansivity function might be defined by the overall tertiary topology of the protein fold; a hypothesis that was supported by the data for the ancestral Trx. Also, the αN values were slightly different even for proteins with the same topology (Trx).
Description
August 2016
School of Science
Department
Dept. of Chemistry and Chemical Biology
Publisher
Rensselaer Polytechnic Institute, Troy, NY
Relationships
Rensselaer Theses and Dissertations Online Collection
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