Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones

To help cells cope with protein misfolding and aggregation, Hsp70 molecular chaperones selectively bind a variety of sequences ("selective promiscuity"). Statistical analyses from substrate-derived peptide arrays reveal that DnaK, the E. coli Hsp70, binds to sequences containing three to f...

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Bibliographic Details
Main Authors:	Chen, J. (Author), Clerico, E.M (Author), English, C.A (Author), Gierasch, L.M (Author), Nordquist, E.B (Author), Sherman, W. (Author)
Format:	Article
Language:	English
Published:	Public Library of Science 2021
Subjects:	Article binding site Binding Sites biology chemical phenomena Computational Biology dnaK protein, E coli Escherichia coli protein Escherichia coli Proteins heat shock protein 70 HSP70 Heat-Shock Proteins hydrogen bond Hydrophobic and Hydrophilic Interactions metabolism molecular dynamics Molecular Dynamics Simulation molecular physics peptide microarray physical phenomena Physical Phenomena prediction procedures protein aggregation protein binding Protein Binding protein conformation Protein Conformation protein DnaK protein domain Protein Domains protein expression protein misfolding protein protein interaction
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Physics-based modeling provides predictive understanding of selectively promiscuous substrate binding by Hsp70 chaperones

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