Making sense of the past: hyperstability of ancestral thioredoxins explained by free energy simulations
Author:
Affiliation:
1. Área de Farmacología
2. Departamento de Ciencias Biomédicas
3. Facultad de Medicina y Ciencias de la Salud
4. Universidad de Alcalá
5. E-28805 Alcalá de Henares
Abstract
Thioredoxin (Trx), a small and globular protein, is present in all kinds of organisms, from Archea to higher mammals.
Publisher
Royal Society of Chemistry (RSC)
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Link
http://pubs.rsc.org/en/content/articlepdf/2017/CP/C7CP03659K
Reference22 articles.
1. Engineering ancestral protein hyperstability
2. Single-molecule paleoenzymology probes the chemistry of resurrected enzymes
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4. Crystal structure of thioredoxin from Escherichia coli at 1.68 Å resolution
5. Thioredoxin structure and mechanism: conformational changes on oxidation of the active-site sulfhydryls to a disulfide
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1. Thr-to-Ala Mutation Leads to a Larger Aromatic Pair and Reduced Packing Density in α1,α3-Helices during Thioredoxin Cold Adaptation;ACS Omega;2024-02-24
2. Structural conservation in the glutathione binding in Sphingomonas sp. glutaredoxin Grx3 and variations for cold adaptation;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2024-01
3. Unraveling the roles of aromatic cluster side-chain interactions on the structural stability and functional significance of psychrophilic Sphingomonas sp. glutaredoxin 3;PLOS ONE;2023-08-31
4. Resurrecting Enzymes by Ancestral Sequence Reconstruction;Methods in Molecular Biology;2021-11-24
5. Functional analyses of ancestral thioredoxins provide insights into their evolutionary history;Journal of Biological Chemistry;2019-09
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