Biosynthetic Protein Folding and Molecular Chaperons
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Summary
The review summarizes available data on the early events of nascent chain folding, as well as on later advanced steps, including formation of elements of native structure, in the context of energy landscapes.
- Type
- review
- Published
- 2022-01-01
- Cited by
- 6
- References
- 147
- OpenAlex
- https://openalex.org/W4210423528
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:246433251
Keywords
Protein folding, Folding (DSP implementation), Computational biology, Biology, Chemistry
References
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- Protein memory through altered folding mediated by intramolecular chaperones
- Ribosomes pause at specific sites during synthesis of membrane-bound chloroplast reaction center protein D1.
- Cotranslational Protein Folding inside the Ribosome Exit Tunnel
- A quantitative assessment of the role of the chaperonin proteins in protein folding in vivo
- The relationship between synonymous codon usage and protein structure.
Cited by
- GroEL—A Versatile Chaperone for Engineering and a Plethora of Applications
- Folding of the nascent polypeptide chain of a histidine phosphocarrier protein in vitro.
- Characterization of Escherichia coli chaperonin GroEL as a ribonuclease.
- Closing the Loop in the Carbon Cycle: Enzymatic Reactions Housed in Metal–Organic Frameworks for CO2 Conversion to Methanol
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