| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1929820 | Biochemical and Biophysical Research Communications | 2012 | 5 Pages |
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.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Molecular Dynamics simulations of Escherichia coli sHsps IbpA and IbpB. ► Solvent exclusion identified as a critical factor driving heterooligomer formation. ► Mechanism of heat activation of IbpA linked to formation of IbpAIbpB heterooligomer.
