Author

G. Gamiz-Arco

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 4 Approach:experimental assay· 2 Assay:protein structure· 2 Approach:statistical model· 2 Organism:bacteria (other)· 1 Organism:E. coli· 1 Assay:protein sequence· 1 Assay:proteomics· 1

Frequent Co-Authors

B. Ibarra-Molero· 3 shared J. M. Sanchez-Ruiz· 3 shared V. A. Risso· 3 shared D. Petrovic· 2 shared E. A. Gaucher· 2 shared J. A. Gavira· 2 shared A. Ingles-Prieto· 1 shared A. M. Candel· 1 shared

Activity by Year

2019-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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3 shared papersBiophysics

B. Ibarra-Molero

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4 papers

Recent·Most cited

Ancestral versus Modern Substrate Scope in Family-1 Glycosidases

L. I. Gutierrez-Rus, D. Petrovic, P. Schneider, K. Zorn, G. Gamiz-Arco, R. Romero-Zaliz, I. Suarez-Martin, L. De Maria, F. Falcioni, V. A. Risso, M. A. Hayes, J. M. Sanchez-Ruiz

This study compares the substrate scope of a modern and ancestral family-1 glycosidase, finding the ancestral enzyme more efficient with large aglycon-containing flavonoid glycosides.

bioRxiv · Apr 11, 2024Biochemistry

Combining ancestral reconstruction with folding-landscape simulations to engineer heterologous protein expression

G. Gamiz-Arco, V. A. Risso, E. A. Gaucher, J. A. Gavira, A. N. Naganathan, B. Ibarra-Molero, J. M. Sanchez-Ruiz

This study engineers a symbiont thioredoxin for efficient heterologous expression by resurrecting ancestral proteins and optimizing folding rates.

bioRxiv · Jul 16, 2021Biophysics

Novel heme-binding enables allosteric modulation in an ancient TIM-barrel glycosidase

G. Gamiz-Arco, L. Gutierrez-Rus, V. Risso, B. Ibarra-Molero, Y. Hoshino, D. Petrovic, A. Romero-Rivera, B. Seelig, J. Gavira, S. Kamerlin, E. Gaucher, J. Sanchez-Ruiz

This study identifies a heme-binding site in an ancestral glycosidase, showing how heme binding rigidifies the TIM-barrel and enhances catalysis.

bioRxiv · May 27, 2020Biophysics

Non-conservation of folding rates in the thioredoxin family reveals degradation of ancestral unassisted-folding

G. Gamiz-Arco, V. A. Risso, A. M. Candel, A. Ingles-Prieto, M. L. Romero-Romero, E. A. Gaucher, J. A. Gavira, B. Ibarra-Molero, J. M. Sanchez-Ruiz

The paper analyzes folding rates of thioredoxins across species and finds that modern variants fold slower than ancestral ones, suggesting degradation of unassisted folding.

bioRxiv · Oct 3, 2019Biophysics