This title appears in the Scientific Report :
2009
Please use the identifier:
http://dx.doi.org/10.1007/s00018-009-8771-9 in citations.
The perspective of studying multi-domain protein folding
The perspective of studying multi-domain protein folding
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...
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Personal Name(s): | Fitter, J. |
---|---|
Contributing Institute: |
Molekulare Biophysik; ISB-2 |
Published in: | Cellular and molecular life sciences, 66 (2009) S. 1672 - 1681 |
Imprint: |
Basel
Birkhäuser
2009
|
Physical Description: |
1672 - 1681 |
PubMed ID: |
19183848 |
DOI: |
10.1007/s00018-009-8771-9 |
Document Type: |
Journal Article |
Research Program: |
Programm Biosoft |
Series Title: |
Cellular and Molecular Life Sciences
66 |
Subject (ZB): | |
Publikationsportal JuSER |
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. |