| Rebekka M. Wachter Research |
Our laboratory is interested in understanding the
mechanisms of protein self-processing reactions,
known to be essential in the generation of functional
diversity from a common protein scaffold. In the
family of fluorescent proteins, spontaneous
cyclization and oxidation reactions of intrinsic amino
acid residues generate functional diversity from a
common protein scaffold, leading to brightly
fluorescing chromophores with different colors
embedded in the protein’s interior. In a related
project, we are investigating the structural basis of
color evolution in fluorescent proteins, as the same
set of colors appears to have evolved independently
along several different lineages.
Other research areas in our laboratory address the
regulation of carbon fixation in higher plants and
green algae, and the structure and function of M. tb
protein factors involved in pathogenesis.
mechanisms of protein self-processing reactions,
known to be essential in the generation of functional
diversity from a common protein scaffold. In the
family of fluorescent proteins, spontaneous
cyclization and oxidation reactions of intrinsic amino
acid residues generate functional diversity from a
common protein scaffold, leading to brightly
fluorescing chromophores with different colors
embedded in the protein’s interior. In a related
project, we are investigating the structural basis of
color evolution in fluorescent proteins, as the same
set of colors appears to have evolved independently
along several different lineages.
Other research areas in our laboratory address the
regulation of carbon fixation in higher plants and
green algae, and the structure and function of M. tb
protein factors involved in pathogenesis.
Department of Chemistry and Biochemistry
Center for Bioenergy and Photosynthesis
Center for Bioenergy and Photosynthesis
Research Overview
Cerulean GFP belongs to a class of
engineered cyan fluorescent proteins that
bear a tryptophan-derived chromophore.
Recent work from the Wachter lab
suggests that the Cerulean fluorophore
may undergo pH-dependent cis-trans
isomerization in the protein's interior.
engineered cyan fluorescent proteins that
bear a tryptophan-derived chromophore.
Recent work from the Wachter lab
suggests that the Cerulean fluorophore
may undergo pH-dependent cis-trans
isomerization in the protein's interior.