Anastassia Andreevna Vorobieva

The paper demonstrates that negative design, which locally destabilizes β-strands, improves folding efficiency of synthetic transmembrane β-barrels in a cell-free system.

This paper designs stable transmembrane beta-barrel nanopores with tailored sizes and shapes using de novo protein design, achieving conductances ranging from 110 pS to 430 pS.

The paper designs nanomolar binders for diverse small molecules using a pseudocycle-based shape complementarity method, enabling direct conversion into sensing systems.

This study benchmarks ProteinMPNN for designing transmembrane β-barrel proteins, showing it outperforms Franklin2023 with refined inputs and generates sequences suitable for experimental validation.

The paper compares AlphaFold2 and ESMFold in validating de novo protein designs, showing AlphaFold2 better predicts experimental folding success while ESMFold excels in structure prediction from contacts.

This study successfully designs transmembrane beta-barrels from first principles, revealing structural constraints and enabling custom pore design for biotechnology applications.