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Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70
07:14

Escherichia coli -Based Complementation Assay to Study the Chaperone Function of Heat Shock Protein 70

Published on: March 8, 2024

Independent evolution of the core domain and its flanking sequences in small heat shock proteins

Thomas Kriehuber1, Thomas Rattei, Thomas Weinmaier

  • 1Munich Center for Integrated Protein Science and Department Chemie Technische Universität München, Garching, Germany.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|May 27, 2010
PubMed

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Conservation of Protein Domains02:26

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Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Intrinsically Disordered Proteins02:18

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Conserved Binding Sites01:49

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