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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Tác giả chính: Christopher J., Reed, Hunter, Lewis
Ngôn ngữ:English
Năm xuất bản: United Kingdom 2018
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spelling 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
institution Trung tâm Học liệu Đại học Quảng Bình (Dspace)
collection Trung tâm Học liệu Đại học Quảng Bình (Dspace)
language English
topic Microbiology
spellingShingle Microbiology
Christopher J., Reed
Hunter, Lewis
Protein Adaptations in Archaeal Extremophiles
description 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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