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Updated: Aug 9, 2026

4D Imaging of Protein Aggregation in Live Cells
Published on: April 5, 2013
Protein folding in the cell: molecular chaperones pave the way
1Cellular Biochemisty and Biophysics Program, Memorial Sloan Kettering Cancer Center, New York, NY 10021, USA.
Abstract:
In vitro, many unfolded polypeptides are able to fold to the native state spontaneously, indicating that the amino acid sequence of a protein contains all the information necessary to specify its three-dimensional conformation. It had been assumed that protein folding in vivo also generally occurs in a spontaneous process. This view has changed only recently due to the discovery of a number of proteins, now commonly called 'molecular chaperones', which are essential for cellular protein folding and occur ubiquitously in eubacteria, archaebacteria and in eukaryotic cells.
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