Search Results - "proteins"

Chaperone mechanisms in cellular protein folding

Table of Contents: “…Contents: The effect of protein aggregation on productive protein folding -- The function of GroEL and GroES as a folding cage for proteins -- Changes in energy landscape within the folding cage -- Cooperation of different chaperone systems in folding pathways: Hsp70 and chaperonins -- Binding of the Hsp70 homologue protein, DnaK, to newly-synthesized polypeptides -- The role of chaperone mechanisms in toxicity suppression of misfolded disease causing proteins -- Potential uses of the chaperone mechanisms in disease therapeutics.…”
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Series (Molecular chaperones)
Series (Protein folding)

Chaperone mechanisms in cellular protein folding

Table of Contents: “…Contents: The effect of protein aggregation on productive protein folding -- The function of GroEL and GroES as a folding cage for proteins -- Changes in energy landscape within the folding cage -- Cooperation of different chaperone systems in folding pathways: Hsp70 and chaperonins -- Binding of the Hsp70 homologue protein, DnaK, to newly-synthesized polypeptides -- The role of chaperone mechanisms in toxicity suppression of misfolded disease causing proteins -- Potential uses of the chaperone mechanisms in disease therapeutics.…”
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Series (Molecular chaperones)
Series (Protein folding)

Chaperone mechanisms in cellular protein folding

Table of Contents: “…Contents: The effect of protein aggregation on productive protein folding -- The function of GroEL and GroES as a folding cage for proteins -- Changes in energy landscape within the folding cage -- Cooperation of different chaperone systems in folding pathways: Hsp70 and chaperonins -- Binding of the Hsp70 homologue protein, DnaK, to newly-synthesized polypeptides -- The role of chaperone mechanisms in toxicity suppression of misfolded disease causing proteins -- Potential uses of the chaperone mechanisms in disease therapeutics.…”
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Series (Molecular chaperones)
Series (Protein folding)

The interaction network of the GroEL chaperonin

Table of Contents: “…Contents: De novo protein folding and proteome maintenance critically depend on molecular chaperones -- Transitions during protein folding -- Chaperone assisted protein folding -- Productive protein folding is often competed by aggregation -- Reconstitution of GroEL-assisted folding -- GroEL and GroES function as a folding cage for proteins up to 60 kDa -- GroEL structure -- Which proteins need GroEL/GroES for folding? …”
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The interaction network of the GroEL chaperonin

Table of Contents: “…Contents: De novo protein folding and proteome maintenance critically depend on molecular chaperones -- Transitions during protein folding -- Chaperone assisted protein folding -- Productive protein folding is often competed by aggregation -- Reconstitution of GroEL-assisted folding -- GroEL and GroES function as a folding cage for proteins up to 60 kDa -- GroEL structure -- Which proteins need GroEL/GroES for folding? …”
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Series

The interaction network of the GroEL chaperonin

Table of Contents: “…Contents: De novo protein folding and proteome maintenance critically depend on molecular chaperones -- Transitions during protein folding -- Chaperone assisted protein folding -- Productive protein folding is often competed by aggregation -- Reconstitution of GroEL-assisted folding -- GroEL and GroES function as a folding cage for proteins up to 60 kDa -- GroEL structure -- Which proteins need GroEL/GroES for folding? …”
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