کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1929820 | 1050475 | 2012 | 5 صفحه PDF | دانلود رایگان |
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.
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► 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.
Journal: Biochemical and Biophysical Research Communications - Volume 420, Issue 3, 13 April 2012, Pages 639–643