B. Ibarra-Molero

Active site center redesign increases protein stability preserving catalysis

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

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

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

Evidence for a role of phenotypic mutations in virus adaptation

This study shows that virus adaptation can occur through phenotypic mutations rather than genetic mutations in the viral DNA polymerase.

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

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

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

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