Cellular and Molecular Life Sciences

, Volume 66, Issue 10, pp 1672–1681 | Cite as

The perspectives of studying multi-domain protein folding

  • J. FitterEmail author


Most of fundamental studies on protein folding have been performed with small globular proteins consisting of a single domain. In vitro many of these proteins are well characterized by a reversible two-state folding scheme. However, the majority of proteins in the cell belong to the class of larger multi-domain proteins that often unfold irreversibly under in vitro conditions. This makes folding studies difficult or even impossible. In spite of these problems for many multi-domain proteins, folding has been investigated by classical refolding. Co-translational folding of nascent polypeptide chains when synthesized by ribosomes has also been studied. Single molecule techniques represent a promising approach for future studies on the folding of multi-domain proteins, and tremendous advances have been made in these techniques in recent years. In particular, fluorescence-based methods can contribute significantly to an understanding of the fundamental principles of multi-domain protein folding.


Irreversible unfolding protein aggregation domain interaction co-translational folding single molecule studies fluorescence correlation spectroscopy 


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Copyright information

© Birkhäuser Verlag, Basel 2009

Authors and Affiliations

  1. 1.Research Center Jülich, ISB-2: Molecular BiophysicsJülichGermany

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