Jaenicke, Rainer (1998) Protein self-organization in vitro and in vivo: Partitioning between physical biochemistry and cell biology. BIOLOGICAL CHEMISTRY, 379 (3). pp. 237-243. ISSN 1431-6730, 1437-4315
Full text not available from this repository.Abstract
Protein folding is a hierarchical process, driven by the accumulation of increments of free energy from local interactions between neighboring residues, secondary structural elements, domains and subunits, The latter represent independent folding units. Thus, the folding kinetics divide into the collapse of sub-domains and domains and their merging to form the compact tertiary fold. In proceeding to oligomeric proteins, docking of structured monomers is the final step, In agreement with this mechanism, in vitro experiments show that the overall mechanism of folding and association obeys uni-bimolecular kinetics with aggregation as a competing side reaction, In vivo, accessory proteins serve to shift the kinetic partitioning between assembly and misassembly toward the native state, So far, co- and post-translational protein folding in the cell has been withstanding a detailed kinetic analysis, Despite obvious differences between the crowded cytosol and optimized in vitro folding conditions, the general mechanism of protein self-organization within and without the cell seems to be similar, Effects of solvent parameters on the rate and mode of protein folding are less significant than predicted. Addition of small ligands and compatible solutes allow nucleation steps and viscosity effects to be analyzed. The absence of chimeras after synchronous in vitro reconstitution of oligomeric enzymes proves subunit interactions to be highly specific.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | LACTATE-DEHYDROGENASE; THERMOTOGA-MARITIMA; DISULFIDE BONDS; FREE SYSTEM; IN-VITRO; RECONSTITUTION; AGGREGATION; STABILITY; ENZYME; COMPETITION; aggregation; association; chaperones; folding; in vitro; in vivo |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Petra Gürster |
| Date Deposited: | 07 Nov 2024 09:30 |
| Last Modified: | 07 Nov 2024 09:30 |
| URI: | https://pred.uni-regensburg.de/id/eprint/50028 |
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