Author

M. Costas

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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Biochemistry· 2

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Organism:bacteria (other)· 1 Approach:deep learning· 1 Approach:experimental assay· 1 Approach:statistical model· 1

Frequent Co-Authors

A. Rodriguez-Romero· 2 shared D. A. Fernandez-Velasco· 2 shared D.-A. Silva· 2 shared S. Romero-Romero· 2 shared A. Sosa-Peinado· 1 shared B. Höcker· 1 shared C. Tapia· 1 shared D. Baker· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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2 shared papersBiochemistry

A. Rodriguez-Romero

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2 papers

Recent·Most cited

Thermodynamic and kinetic analysis of the LAO binding protein and its isolated domains reveal non-additivity in stability, folding, and function

R. Vergara, T. Berrocal, E. I. Juarez Mejia, S. Romero-Romero, I. Velaquez-Lopez, N. Pulido, H. A. Lopez Sanchez, D.-A. Silva, M. Costas, A. Rodriguez-Romero, R. Rodriguez-Sotres, A. Sosa-Peinado, D. A. Fernandez-Velasco

This study analyzes the thermodynamic and kinetic properties of LAO and its domains, revealing non-additive effects in stability, folding, and function.

The FEBS Journal · May 29, 2023Peer-reviewedBiochemistry

The stability landscape of de novo TIM barrels explored by a modular design approach

S. Romero-Romero, M. Costas, D.-A. Silva, S. Kordes, E. Rojas-Ortega, Y. Guerra, C. Tapia, S. Shanmugaratnam, A. Rodriguez-Romero, D. Baker, B. Höcker, D. A. Fernandez-Velasco

This study designs a family of stable de novo TIM barrels with diverse thermodynamic properties and identifies epistatic effects influencing their stability.

bioRxiv · Sep 29, 2020Biochemistry