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A chaperonin protein, GroEL, has a more complex mechanism than was thought before

by Staff July 10, 2018
July 10, 2018 78 views

Scientists have studied molecular interactions in the chaperonin protein GroEL. GroEL is alternately bound and unbound by a co-chaperonin, GroES. Against expectations, the ‘football’ complex — where two GroES units cap the cylindrical GroEL at either end — was roughly as prevalent as the single-bound ‘bullet’ complex. This implies that negative allosteric interactions preventing double-binding of GroEL sometimes fail, and the double-bound complex plays an active role in protein folding.

Source: sciencedaily.com

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