%0 Journal Article
%A Fitter, J.
%T The perspective of studying multi-domain protein folding
%J Cellular and molecular life sciences
%V 66
%@ 1420-682X
%C Basel
%I Birkhäuser
%M PreJuSER-4685
%P 1672 - 1681
%D 2009
%Z Record converted from VDB: 12.11.2012
%X 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.
%K Animals
%K Humans
%K Models, Molecular
%K Protein Folding
%K Protein Structure, Tertiary
%K Proteins: chemistry
%K Spectrometry, Fluorescence
%K Proteins (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:19183848
%U <Go to ISI:>//WOS:000268003600004
%R 10.1007/s00018-009-8771-9
%U https://juser.fz-juelich.de/record/4685