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Converging concepts of protein folding in vitro and in vivo

Nature Structural & Molecular Biology volume 16, pages 574–581 (2009)Cite this article

Abstract

Most proteins must fold into precise three-dimensional conformations to fulfill their biological functions. Here we review recent concepts emerging from studies of protein folding in vitro and in vivo, with a focus on how proteins navigate the complex folding energy landscape inside cells with the aid of molecular chaperones. Understanding these reactions is also of considerable medical relevance, as the aggregation of misfolding proteins that escape the cellular quality-control machinery underlies a range of debilitating diseases, including many age-onset neurodegenerative disorders.

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Figure 1: Energy landscape scheme of protein folding and aggregation.
Figure 2: Chaperone mechanism in promoting folding through kinetic partitioning.
Figure 3: Protein folding in the cytosol.
Figure 4: Structure and function of Trigger factor (TF).
Figure 5: Hsp70 system.
Figure 6: The GroEL-GroES chaperonin.

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Acknowledgements

Work in our laboratory is supported by the Max-Planck-Gesellschaft, the Deutsche Forschungsgemeinschaft, The European Commission, The Körber Foundation and the Ernst-Jung-Foundation.

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  1. Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Martinsried, Germany

    F Ulrich Hartl & Manajit Hayer-Hartl

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Correspondence to F Ulrich Hartl or Manajit Hayer-Hartl.

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Hartl, F., Hayer-Hartl, M. Converging concepts of protein folding in vitro and in vivo. Nat Struct Mol Biol 16, 574–581 (2009). https://doi.org/10.1038/nsmb.1591

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