Molecular mechanisms of adaptation to high hydrostatic pressure

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Authors
Avagyan, Samvel
Issue Date
2021-05
Type
Electronic thesis
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Language
ENG
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Biology
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Abstract
The effect of pressure on the thermodynamic stability of biological macromolecules is directly related to the molecules’ change in volume upon denaturation. This suggest that if a macromolecule such as a protein, upon transition from its native state to its unfolded state, experiences a volume change then it is susceptible to the effects of pressure; however, pressure effects can be stabilizing or destabilizing and the sign of the volume change determines which effect will be imparted onto the molecule. If the sign of the volume change is negative (meaning that the native state has a larger volume than the unfolded state) then high pressure will denature the molecule. However, if the sign is positive (meaning that the native state has a smaller volume than the unfolded state) then the molecule will be stabilized by high pressure. This phenomenon can also be applied any two-state biological process such as oligomerization, ligand-binding, complex formation, and even enzymatic reactions, which experience a change in volume upon transition. In the case of these quaternary interactions, if the associated complex has a larger volume than the sum of the volume of the dissociated components, then high pressure will destabilize the complex; however, if the opposite is true (the complex has a smaller volume than the sum of its components) then high pressure will stabilize complex formation. Based on this thermodynamic description of the effect of pressure on biological macromolecules, we set out to understand if piezophilic organisms, when compared to non-piezophilic organisms, may have altered the volumetric properties of their macromolecules and macromolecular complexes in order to withstand the denaturing effects of high hydrostatic pressure.
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May 2021
School of Science
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Rensselaer Polytechnic Institute, Troy, NY
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