A comparison of the folding characteristics of free and ribosome‐tethered polypeptide chains using limited proteolysis and mass spectrometry
Author:
Affiliation:
1. Astbury Centre for Structural Molecular BiologySchool of Molecular and Cellular Biology, University of LeedsLeeds LS2 9JT United Kingdom
2. Department of BiologyUniversity of Konstanz78457Konstanz Germany
Funder
Human Frontiers Science Project
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.2702
Reference34 articles.
1. Principles that Govern the Folding of Protein Chains
2. Energy landscapes of functional proteins are inherently risky
3. Protein folding on the ribosome
4. The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins
5. The Ribosome Can Prevent Aggregation of Partially Folded Protein Intermediates: Studies Using the Escherichia coli Ribosome
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