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Converging concepts of protein folding in vitro and in vivo

F Ulrich Hartl1, Manajit Hayer-Hartl

  • 1Max Planck Institute of Biochemistry, Department of Cellular Biochemistry, Martinsried, Germany. uhartl@biochem.mpg.de

Nature Structural & Molecular Biology
|June 4, 2009
PubMed

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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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