The Functional Differences between the GroEL Chaperonin of <i>Escherichia coli</i> and the HtpB Chaperonin of <i>Legionella pneumophila</i> Can Be Mapped to Specific Amino Acid Residues
Group I chaperonins are a highly conserved family of essential proteins that self-assemble into molecular nanoboxes that mediate the folding of cytoplasmic proteins in bacteria and organelles. GroEL, the chaperonin of <i>Escherichia coli</i>, is the archetype of the family. Protein foldi...
Main Authors: | Karla N. Valenzuela-Valderas, Gabriel Moreno-Hagelsieb, John R. Rohde, Rafael A. Garduño |
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Format: | Article |
Language: | English |
Published: |
MDPI AG
2021-12-01
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Series: | Biomolecules |
Subjects: | |
Online Access: | https://www.mdpi.com/2218-273X/12/1/59 |
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