Author

M. L. 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

Signature Assays, Organisms & Methods

Click to filter · or open tag

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

Frequent Co-Authors

B. Ibarra-Molero· 2 shared A. Ingles-Prieto· 1 shared A. M. Candel· 1 shared E. A. Gaucher· 1 shared G. Gamiz-Arco· 1 shared H. Garcia-Seisdedos· 1 shared J. A. Gavira· 1 shared J. M. Sanchez-Ruiz· 1 shared

Activity by Year

2019-2022 · peak 1/yr

Co-Author Collaboration Network

9 top collaborators · 29 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

2 shared papersBiophysics

B. Ibarra-Molero

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

BiophysicsbioRxivJan 31, 2022

Active site center redesign increases protein stability preserving catalysis

M. L. Romero-Romero, H. Garcia-Seisdedos, B. Ibarra-Molero

This paper redesigns the active site of thioredoxin to increase protein stability while preserving catalytic activity through surface mutations.

DOI 10.1002/pro.4417

protein structurestatistical model

𝕏 PostBluesky

BiophysicsbioRxivOct 3, 2019

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

G. Gamiz-Arco, V. A. Risso, A. M. Candel…·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.

DOI 10.1042/bcj20190739

bacteria (other)protein structure

𝕏 PostBluesky