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Conformations of co-translational folding intermediates
Michael S Evans1, Thomas F Clarke, Patricia L Clark
1Department of Chemistry and Biochemistry, University of Notre Dame, 251 Nieuwland Science Hall, Notre Dame, IN 46556, USA.
Protein and Peptide Letters
|February 23, 2005
Summary
This review explores how proteins fold inside living cells, focusing on early folding stages during ribosome synthesis. It discusses cellular challenges like aggregation and crowding that impact protein folding.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- In vitro studies provide foundational knowledge of protein folding.
- Understanding in vivo protein folding remains a significant challenge.
- Nascent polypeptides synthesized by the ribosome are key subjects.
Purpose of the Study:
- To review current knowledge on early in vivo protein folding intermediates.
- To discuss conformations adopted by nascent polypeptides during ribosomal synthesis.
- To explore challenges of protein folding within the cellular environment.
Main Methods:
- Literature review of in vivo protein folding studies.
- Analysis of nascent polypeptide conformations.
- Discussion of cellular factors influencing folding.
Main Results:
- Identified earliest in vivo folding intermediates as conformations of nascent polypeptides.
- Highlighted the ribosome's role in initiating protein folding.
- Detailed challenges including off-pathway aggregation and macromolecular crowding.
Conclusions:
- In vivo protein folding is complex and distinct from in vitro conditions.
- Nascent polypeptide conformations are critical early folding events.
- Cellular environment presents significant hurdles to successful protein folding.