Science · 1990 · 224 citations · 37 references
Life SciencesBiochemistryPlant BiologyPhotosynthesisPlant Molecular BiologyProtein FoldingChaperone-assisted FoldingChaperone-mediated FoldingChloroplast BiochemistryChloroplast BiologyMolecular ChaperonesPhotosynthesis BiochemistryCarbon DioxideChaperone-assisted AssemblyChaperone-mediated AssemblyChaperone-mediated InteractionsChaperone-substrate InteractionsChaperone-substrate RecognitionProtein Self-assemblyStructural Biology Of Chaperones
Molecular chaperones are a family of unrelated proteins found in all types of cell. They mediate the correct assembly of other polypeptides, but are not components of the mature assembled structures. Chaperones function by binding specifically to interactive protein surfaces that are exposed transiently during many cellular processes and so prevent them from undergoing incorrect interactions that might produce nonfunctional structures. The concept of molecular chaperones originated largely from studies of the chloroplast enzyme rubisco, which fixes carbon dioxide in plant photosynthesis; the function of chaperones forces a rethinking of the principle of protein self-assembly.
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Principles that Govern the Folding of Protein Chains
Christian B. Anfinsen · Science · 1973 · 7.1K citations
Rapid and Sensitive Protein Similarity Searches
David J. Lipman, William R. Pearson · Science · 1985 · 4.1K citations
Homologous plant and bacterial proteins chaperone oligomeric protein assembly
Sean M. Hemmingsen, Carol A. Woolford, Saskia M. van der Vies et al. · Nature · 1988 · 1.3K citations