Characterisation of denatured states of sensory rhodopsin II by solution-state NMR
research article
PhD
This paper establishes sensory rhodopsin II as a model for membrane protein folding by using NMR to measure the changes to different residues upon unfolding
This is a partner paper to the other sensory rhodopsin paper. Yi-Lei was an experimental powerhouse for these papers, and the manuscript goes through the results in extraordinary detail. In my thesis, I used PCA to show that the general trends in chemical shift changes could be related to the concentration of SDS used, but this didn’t make it into the paper.