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THERMODYNAMIC AND KINETIC ASPECTS OF THE FOLDING AND SELFASSEMBLY OF PROTEINS
Jaenicke, Rainer
Jaenicke, Rainer
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Issue Date
1988
Submitted date
2023-10-25
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Abstract
The acquisition of the spatial structure of proteins may be described as a hierarchical condensation reaction. Starting from next-neighbor interac tions (involved in secondary structure formation), the native tertiary and quaternary structure are generated by the merging and docking of domains and subunits. The overall kinetics of the folding and assembly of multi subunit oligomeric proteins consist of consecutive unimolecular and bimo lecular steps which may be distinguished by concentration-dependent recon stitution experiments. In order to reach the native state, both folding and association must be tuned such that the formation of the correct subunit recognition sites precedes association. Beyond a limiting concentration, "wrong aggregation” (in vitro) or precipitation of "inclusion bodies" (in overexpressing strains of bacteria) are found to outrun proper structure formation. Other variables determining the yield and rate of in vitro reconstitution are the temperature, pH, ionic strength and specific ligands. Apart from the physi co-chemical parameters, folding in vivo may be affected by codon usage, amino-acid pools and genome organization.
Citation
Advances in protein design, 3 - 11
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Book chapter
conference paper
conference paper
Language
en
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GBF monographs ; Volume 12
ISSN
0930-4320
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ISBN
3527280243
0895739534
0895739534
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Attribution-NonCommercial-ShareAlike 4.0 International