PMID:22450329
| Citation |
Healy, EF (2012) A model for heterooligomer formation in the heat shock response of Escherichia coli. Biochem. Biophys. Res. Commun. 420:639-43 |
|---|---|
| Abstract |
Small heat shock proteins (sHsp) are widely distributed molecular chaperones that bind to misfolded proteins to prevent irreversible aggregation and aid in refolding to a competent state. The sHsps characterized thus far all contain a conserved α-crystallin, and variable N- and C-termini critical for chaperone activity and oligomerization. The Escherichia coli sHsps IbpA and IbpB share 48% sequence homology, are induced by heat shock and oxidative stress, and each requires the presence of the other to effect protein protection. Molecular Dynamics (MD) simulations of homology-modeled monomers and heterooligomers of these sHsps identify a possible mechanism for cooperation between IbpA and IbpB. |
| Links |
PubMed Online version:10.1016/j.bbrc.2012.03.054 |
| Keywords |
Escherichia coli/metabolism; Escherichia coli/physiology; Escherichia coli Proteins/chemistry; Heat-Shock Proteins/chemistry; Heat-Shock Response; Models, Chemical; Molecular Dynamics Simulation; Protein Folding; Protein Multimerization; Protein Structure, Secondary |
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