Josef Wachtveitl

This paper computationally designs light-responsive proteins that undergo conformational changes upon light activation, enabling precise control of biological functions.

This study computationally designs soluble analogues of animal and microbial rhodopsins, showing they are well-folded, thermostable, and retain retinal photocycle functionality.

The paper identifies a doxycycline-binding aptamer with exceptional regulatory properties in yeast and human cells, revealing a unique structural mechanism and validating its effectiveness through experimental methods.

The paper presents cryo-EM structures of FArhodopsin and proteorhodopsin, showing no retinal binding despite conserved lysine and similar fold to retinal-binding rhodopsins, with mutations identified that prevent retinal binding.

The paper characterizes CryoRhodopsins from cold environments, revealing their dual functionality and structural adaptations to low temperatures.

The paper identifies a new subgroup of light-driven sodium pumps with an additional glutamic acid residue that reduces pH sensitivity for sodium transport.

The paper captures the release of a photopharmacological drug from tubulin using time-resolved serial crystallography and shows how ligand release triggers conformational changes.