Author

S. Romero-Romero

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

Biology Disciplines

Click to filter author papers

Biochemistry· 3 Biophysics· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:protein folding & dynamics· 4 Assay:protein structure· 4 Approach:experimental assay· 3 Approach:statistical model· 2 Organism:bacteria (other)· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1

Frequent Co-Authors

B. Höcker· 3 shared A. Rodriguez-Romero· 2 shared D. A. Fernandez-Velasco· 2 shared D.-A. Silva· 2 shared M. Costas· 2 shared A. A. Jalan· 1 shared A. Sosa-Peinado· 1 shared C. Tapia· 1 shared

Activity by Year

2020-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiochemistry

B. Höcker

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

BiophysicsbioRxivPreprintSep 29, 2023

Hydrophobic Clusters Direct Folding of a Synthetic Chimeric Protein

A. A. Jalan, L. Hassine, S. Romero-Romero…·B. Höcker

This study investigates how hydrophobic clusters influence the folding and stability of a synthetic chimeric protein made from fragments of two different proteins.

DOI 10.1101/2023.09.29.560087

protein structureprotein sequence

𝕏 PostBluesky

BiochemistrybioRxivMay 30, 2023

Retracing the evolution of a modern periplasmic binding protein

F. Michel, S. Romero-Romero, B. Höcker

This study reconstructs a single-lobed progenitor of a periplasmic binding protein by deconstructing a modern RBP, showing that recombination of its lobes restores function and structure.

DOI 10.1002/pro.4793

protein structureexperimental assay

𝕏 PostBluesky

BiochemistryThe FEBS JournalPeer-reviewedMay 29, 2023

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…·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.

DOI 10.1111/febs.16819

bacteria (other)protein structure

𝕏 PostBluesky

BiochemistrybioRxivSep 29, 2020

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

S. Romero-Romero, M. Costas, D.-A. Silva…·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.

DOI 10.1016/j.jmb.2021.167153

protein structuredeep learning

𝕏 PostBluesky