What is it about?
In the article, we identify two, topologically distinct folding pathways of UCH-L proteins. We analyze the dependence of the pathways on the conditions (confinement, temperature etc) and relate the data to the experiment.
Featured Image
Why is it important?
The Ubiquitine C-terminal Hydrolase (UCH) is the most common protein the human brain. Its folding pathway includes the oligomerization-prone intermediate products of unknown structure. The study of the folding pathway may therefore lead to understanding of the oligomerization of the protein, and, as a consequence, lead to understanding of the origins of neurodegenerative diseases.
Perspectives
The article is the first step describing the folding pathway of the protein. It will be continued in more in-depth analysis of the pathway with subsequent determination of the structures of the folding pathway intermediate products.
Pawel Dabrowski-Tumanski
University of Warsaw
Read the Original
This page is a summary of: The exclusive effects of chaperonin on the behavior of proteins with 52 knot, PLoS Computational Biology, March 2018, PLOS,
DOI: 10.1371/journal.pcbi.1005970.
You can read the full text:
Contributors
The following have contributed to this page
