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| Paper: |
Crystallization of Extremophile Rubredoxins to Aid Temperature Dependent Flexibility Measurements |
| Volume: |
540, Compendium of Undergraduate Research in Astronomy and Space Science |
| Page: |
66 |
| Authors: |
Trenton Turpin; Celeste Paerels; Tzanko Doukov; Stephen Cramer |
| DOI: |
10.26624/HPOV7556 |
| Abstract: |
Extremophiles are organisms that live and grow under extreme conditions. Such conditions include extreme cold, extreme heat, and extreme pressure. Understanding the viability of life under these stressors has applications for human health, biotechnology, bioremediation, and the search for life beyond our planet. Understanding the dynamics of proteins in extremophiles is key to understanding their functions and their broader applications. One proposed framework for understanding extremophile protein dynamics is the corresponding states hypothesis. This is the idea that the flexibility of homologous proteins from different extremophilic organisms will be comparable at their respective growth temperatures. However, the hypothesis is not universally accepted as evidence is contradictory. This conflicted body of evidence calls for a comprehensive experimental review using a variety of methods. Our study aims to contribute to this body of evidence by including X-ray diffraction, small-angle X-ray scattering, and molecular dynamics measurements at a range of temperatures on multiple extremophile rubredoxins. We utilized rubredoxin samples of two hyperthermophiles, Pyrococcus furiosus and Pyrococcus yayanosii, and two psychrophiles, Polaromonas glacialis and Polaromonas glacialis Eur3. |
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