معرفی
Jaap Broos investigates protein structure and function using biochemical and biophysical methodologies, with a focus on tryptophan fluorescence and phosphorescence. His work employs Trp analogs like 7-azatryptophan and 5-fluorotryptophan to study proteins such as the mannitol transporter (EIImtl) from E. coli, domain 1 of transhydrogenase from Rhodospirillum rubrum, and LysM domains from Lactococcus lactis.
Research highlights include developing a Lactococcus lactis expression system for Trp analog incorporation, enabling studies with reduced structural disruption. His team discovered that 5-fluorotryptophan exhibits monoexponential fluorescence decay, simplifying distance calculations in RET experiments. Collaborations with Prof. Callis (Montana State University) and Prof. Buma (Amsterdam University) have advanced theoretical and experimental understanding of Trp fluorescence dynamics.
Key projects involve mapping the mannitol binding site in EIImtl using azi-mannitol and elucidating the 1Lb emission state of Trp in rigid protein environments. Publications span journals like Methods Mol. Biol., J. Am. Chem. Soc., and Biophys. J., reflecting interdisciplinary work in protein spectroscopy and engineering.
