2000Current Opinion in MicrobiologyOpen access

Protein folding and unfolding by Escherichia coli chaperones and chaperonins

Max E. Gottesman, Wayne A. Hendrickson

Open full text 44 citations

Abstract

The folding of proteins from their initial unstructured state to their mature form has long been known to be promoted by other proteins known as chaperones and chaperonins. Recent biochemical and structural discoveries have provided dramatic insight into how these folding proteins work. This review will discuss these findings and suggest future experimental directions.

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What this paper is about

The folding of proteins from their initial unstructured state to their mature form has long been known to be promoted by other proteins known as chaperones and chaperonins. Recent biochemical and structural discoveries have provided dramatic insight into how these folding proteins work. This review will discuss these findings and suggest future experimental directions.

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Available abstract

The folding of proteins from their initial unstructured state to their mature form has long been known to be promoted by other proteins known as chaperones and chaperonins. Recent biochemical and structural discoveries have provided dramatic insight into how these folding proteins work. This review will discuss these findings and suggest future experimental directions.

Key concepts: Chaperonin, Protein folding, Biology, Chaperone (clinical), Folding (DSP implementation), Escherichia coli, Co-chaperone, Computational biology

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