کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1929820 1050475 2012 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A model for heterooligomer formation in the heat shock response of Escherichia coli
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
A model for heterooligomer formation in the heat shock response of Escherichia coli
چکیده انگلیسی

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.

Figure optionsDownload 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.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 420, Issue 3, 13 April 2012, Pages 639–643
نویسندگان
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