Protein Adaptations in Archaeal Extremophiles
Extremophiles, especially those in Archaea, have a myriad of adaptations that keep their cellular proteins stable and active under the extreme conditions in which they live. Rather than having one basic set of adaptations that works for all environments, Archaea have evolved separate protein feature...
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United Kingdom
2018
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oai:localhost:DHQB_123456789-38242018-10-22T08:43:39Z Protein Adaptations in Archaeal Extremophiles Christopher J., Reed Hunter, Lewis Microbiology Extremophiles, especially those in Archaea, have a myriad of adaptations that keep their cellular proteins stable and active under the extreme conditions in which they live. Rather than having one basic set of adaptations that works for all environments, Archaea have evolved separate protein features that are customized for each environment. We categorized the Archaea into three general groups to describe what is known about their protein adaptations: thermophilic, psychrophilic, and halophilic. Thermophilic proteins tend to have a prominent hydrophobic core and increased electrostatic interactions to maintain activity at high temperatures. Psychrophilic proteins have a reduced hydrophobic core and a less charged protein surface to maintain flexibility and activity under cold temperatures. Halophilic proteins are characterized by increased negative surface charge due to increased acidic amino acid content and peptide insertions, which compensates for the extreme ionic conditions. While acidophiles, alkaliphiles, and piezophiles are their own class of Archaea, their protein adaptations toward pH and pressure are less discernible. By understanding the protein adaptations used by archaeal extremophiles, we hope to be able to engineer and utilize proteins for industrial, environmental, and biotechnological applications where function in extreme conditions is required for activity. 2018-08-23T02:48:55Z 2018-08-23T02:48:55Z 2018 http://lrc.quangbinhuni.edu.vn:8181/dspace/handle/DHQB_123456789/3824 en United Kingdom |
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English |
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Microbiology |
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Microbiology Christopher J., Reed Hunter, Lewis Protein Adaptations in Archaeal Extremophiles |
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Extremophiles, especially those in Archaea, have a myriad of adaptations that keep their cellular proteins stable and active under the extreme conditions in which they live. Rather than having one basic set of adaptations that works for all environments, Archaea have evolved separate protein features that are customized for each environment. We categorized the Archaea into three general groups to describe what is known about their protein adaptations: thermophilic, psychrophilic, and halophilic. Thermophilic proteins tend to have a prominent hydrophobic core and increased electrostatic interactions to maintain activity at high temperatures. Psychrophilic proteins have a reduced hydrophobic core and a less charged protein surface to maintain flexibility and activity under cold temperatures. Halophilic proteins are characterized by increased negative surface charge due to increased acidic amino acid content and peptide insertions, which compensates for the extreme ionic conditions. While acidophiles, alkaliphiles, and piezophiles are their own class of Archaea, their protein adaptations toward pH and pressure are less discernible. By understanding the protein adaptations used by archaeal extremophiles, we hope to be able to engineer and utilize proteins for industrial, environmental, and biotechnological applications where function in extreme conditions is required for activity. |
author |
Christopher J., Reed Hunter, Lewis |
author_facet |
Christopher J., Reed Hunter, Lewis |
author_sort |
Christopher J., Reed |
title |
Protein Adaptations in Archaeal Extremophiles |
title_short |
Protein Adaptations in Archaeal Extremophiles |
title_full |
Protein Adaptations in Archaeal Extremophiles |
title_fullStr |
Protein Adaptations in Archaeal Extremophiles |
title_full_unstemmed |
Protein Adaptations in Archaeal Extremophiles |
title_sort |
protein adaptations in archaeal extremophiles |
publisher |
United Kingdom |
publishDate |
2018 |
url |
http://lrc.quangbinhuni.edu.vn:8181/dspace/handle/DHQB_123456789/3824 |
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1717292448673169408 |
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9,463379 |