A manuscript with the title “Topological constraints and modular structure in the folding and functional motions of GlpG, an intramembrane protease” has been published in PNAS. This paper uses simulations to investigate the effects of constraining the unfolded ensemble of GlpG in a bilayer on its folding mechanism. Using the detailed folding mechanisms found in this paper, we propose a possible source of the large number of negative phi-values found in our previous experimental work. Otzen lab co-authors include Nicholas P Schafer and Daniel E Otzen. This work is a collaboration with Kresten Lindorff-Larsen at Copenhagen University as well as Ha H Truong and Peter G Wolynes at Rice University.
A manuscript with the title “Cooperative folding of a polytopic α-helical membrane protein involves a compact N-terminal nucleus and nonnative loops” has been published in PNAS. This manuscript describes the most comprehensive phi-value analysis of a membrane protein to-date. Co-authors in the Otzen group include Wojciech Paslawski, Ove K Lillelund, Julie Veje Kristensen, Nicholas P Schafer, and Daniel E Otzen. This work was a collaboration with Rosanna P Baker and Sinisa Urban at Johns Hopkins University.
Nick Schafer will be supported by the Carlsberg Foundation and DFF-FNU for a total of two years to work on a project entitled “Combining experiment and simulation to elucidate folding and stability of the alpha-helical TMP GlpG”.