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Folding and association of oligomeric enzymes

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Abstract

The spontaneous structure formation of oligomeric enzymes consists of the consecutive ‘folding’ and association of the constituent polypeptide chains. Whether catalytic function is an intrinsic property of the folded monomers may be determined using kinetic reconstitution experiments. It is shown that full activity requires association; the correct assembly of subunits depends on their proper folding. The native structure is determined as the kinetically accessible state of lowest free energy.

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Authors and Affiliations

  1. Institut für Biophysik und Physikalische Biochemie der Universität, D-8400, Regensburg

    Rainer Jaenicke

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  1. Rainer Jaenicke
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Dedicated to Dr. Johannes Jaenicke on the occasion of his 90th birthday

Work was supported by the Deutsche Forschungsgemeinschaft and the Fonds der Chemischen Industrie. Excellent technical assistance of Miss Ingrid Heider and stimulating discussions with Drs. R. Rudolph and D.B. Wetlaufer are gratefully acknowledged.

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Jaenicke, R. Folding and association of oligomeric enzymes. Naturwissenschaften 65, 569–577 (1978). https://doi.org/10.1007/BF00364906

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  • DOI: https://doi.org/10.1007/BF00364906

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