Abstract
While in vitro experiments have contributed much to our understanding of protein folding, we know much less about how proteins fold in the more complex environment of the cell. This review summarizes our current knowledge of the earliest in vivo folding intermediates: the conformations adopted by nascent polypeptides during synthesis by the ribosome. The challenges related to successful folding in the cellular environment, including off-pathway aggregation and macromolecular crowding, are also discussed.
Keywords: protein, folding, co-translational, intermediate, misfolding, aggregation, ribosome, translation
Protein & Peptide Letters
Title: Conformations of Co-Translational Folding Intermediates
Volume: 12 Issue: 2
Author(s): Michael S. Evans, Thomas F. Clarke IV and Patricia L. Clark
Affiliation:
Keywords: protein, folding, co-translational, intermediate, misfolding, aggregation, ribosome, translation
Abstract: While in vitro experiments have contributed much to our understanding of protein folding, we know much less about how proteins fold in the more complex environment of the cell. This review summarizes our current knowledge of the earliest in vivo folding intermediates: the conformations adopted by nascent polypeptides during synthesis by the ribosome. The challenges related to successful folding in the cellular environment, including off-pathway aggregation and macromolecular crowding, are also discussed.
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Cite this article as:
Evans S. Michael, Clarke IV F. Thomas and Clark L. Patricia, Conformations of Co-Translational Folding Intermediates, Protein & Peptide Letters 2005; 12 (2) . https://dx.doi.org/10.2174/0929866053005908
DOI https://dx.doi.org/10.2174/0929866053005908 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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