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Updated: Jul 17, 2026

10:56
Assays for the Degradation of Misfolded Proteins in Cells
Published on: August 28, 2016
HAMLET, protein folding, and tumor cell death
K Hun Mok1, Jenny Pettersson, Sten Orrenius
1Trinity College, School of Biochemistry and Immunology, University of Dublin, Dublin 2, Ireland.
Biochemical and Biophysical Research Communications
|January 16, 2007
Summary
No abstract available in PubMed .
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Protein Folding
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Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
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Protein Folding
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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