Maximilian J. L. J. Fürst

This paper introduces a direct enzymatic bioconjugation platform using the flavin transferase ApbE, enabling site-specific conjugation of diverse payloads without intermediate chemical steps.

This paper reprograms a protein ligase into a functional aminoacyl-tRNA synthetase, enabling the incorporation of non-canonical amino acids and post-translational modifications into proteins.

This study evaluates refolding metrics in protein design, showing they are limited by evolutionary information and structural flexibility, reducing their reliability for filtering design candidates.

This paper introduces ADDing, an enzymatic method for attaching click chemistry handles to proteins using ApbE and a dedicated substrate, enabling efficient and versatile bioconjugation.

BoostMut improves thermostability mutation prediction by automating analysis of molecular dynamics simulations and integrating biophysical features.