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| Journal Article | PreJuSER-4685 |
2009
Birkhäuser
Basel
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Please use a persistent id in citations: doi:10.1007/s00018-009-8771-9
Abstract: 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.
Keyword(s): Animals (MeSH) ; Humans (MeSH) ; Models, Molecular (MeSH) ; Protein Folding (MeSH) ; Protein Structure, Tertiary (MeSH) ; Proteins: chemistry (MeSH) ; Spectrometry, Fluorescence (MeSH) ; Proteins ; J ; Irreversible unfolding (auto) ; protein aggregation (auto) ; domain interaction (auto) ; co-translational folding (auto) ; single molecule studies (auto) ; fluorescence correlation spectroscopy (auto)
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