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Article

Effects of modifications near the 2-, 3- and 4-fold symmetry axes on human ferritin renaturation.

The Biochemical journal - 1 Mar 1997

Santambrogio P, Pinto P, Levi S, Cozzi A, Rovida E, Albertini A, Artymiuk P, Harrison P M, Arosio P

Abstract excerpt

Ferritin is a protein of 24 subunits which assemble into a shell with 432 point symmetry. It can be denatured reversibly in acidic guanidine hydrochloride, with the formation of poorly populated renaturation intermediates. In order to increase the accumulation of intermediates and to study the mechanism of ferritin renaturation, we analysed variants of the human ferritin H-chain altered at the N-terminus...

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Identifiers

PMID: 9065764
DOI: 10.1042/bj3220461
PMCID: PMC1218213

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