TY  - JOUR
AU  - Fitter, J.
TI  - The perspective of studying multi-domain protein folding
JO  - Cellular and molecular life sciences
VL  - 66
SN  - 1420-682X
CY  - Basel
PB  - Birkhäuser
M1  - PreJuSER-4685
SP  - 1672 - 1681
PY  - 2009
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Animals
KW  - Humans
KW  - Models, Molecular
KW  - Protein Folding
KW  - Protein Structure, Tertiary
KW  - Proteins: chemistry
KW  - Spectrometry, Fluorescence
KW  - Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:19183848
UR  - <Go to ISI:>//WOS:000268003600004
DO  - DOI:10.1007/s00018-009-8771-9
UR  - https://juser.fz-juelich.de/record/4685
ER  -