The unfolding transition state of ubiquitin with charged residues has higher energy than that with hydrophobic residues
Author:
Affiliation:
1. Department of Chemical Sciences
2. Tata Institute of Fundamental Research
3. Mumbai 400005
4. India
Abstract
The native-state structure and folding pathways of a protein are encoded in its amino acid sequence.
Funder
Department of Atomic Energy, Government of India
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2020/CP/D0CP03876H
Reference55 articles.
1. Funnels, pathways, and the energy landscape of protein folding: A synthesis
2. The Protein-Folding Problem, 50 Years On
3. Engineering more stable proteins
4. Evidence for the principle of minimal frustration in the evolution of protein folding landscapes
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1. Unlocking the unfolded structure of ubiquitin: Combining time-resolved x-ray solution scattering and molecular dynamics to generate unfolded ensembles;The Journal of Chemical Physics;2024-07-15
2. Native Salt Bridges Are a Key Regulator of Ubiquitin’s Mechanical Stability;The Journal of Physical Chemistry B;2022-05-10
3. Ubiquitination at the lysine 27 residue of the Parkin ubiquitin-like domain is suggestive of a new mechanism of Parkin activation;Human Molecular Genetics;2022-03-21
4. K27‐linked noncanonic ubiquitination in immune regulation;Journal of Leukocyte Biology;2021-04-15
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