protein folding
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the process of assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure
Research
99,162 papers- Molecular chaperone functions in protein folding and proteostasis.Annual review of biochemistry · 2013
- Visualizing Protein Folding and Unfolding.Journal of molecular biology · 2019
- Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?International journal of molecular sciences · 2022
- Heterogeneity in Protein Folding and Unfolding Reactions.Chemical reviews · 2022
- Translation Rates and Protein Folding.Journal of molecular biology · 2024
via PubMed
~39 min read
Encyclopedic overview
Protein before and after folding Results of protein folding Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional or active.
The folding of many proteins begins even during the translation of the polypeptide chain. The amino acids interact with each other to produce a well-defined three-dimensional structure, known as the protein's native state. This structure is determined by the amino-acid sequence or primary structure.
Excerpted from Wikipedia’s “protein folding” article, available under the CC BY-SA 4.0 licence.