2nd LINXS Symposium on Integrative Structural Biology

Session

Keynotes and Short talks 6

10 Oct 2019, 16:10

Auditorium (Kulturen)

40. Short Talk 8, Yong Wang - Integrative Ensemble Modeling of a Large Membrane Protein Complex Using Diverse and Ambiguous Information

Yong Wang (University of Copenhagen)

10/10/2019, 16:10

Mitochondria contain approximately 1200 different proteins, 99% of which are synthesized on cytosolic ribosomes and need to be delivered into the right destination through the intermembrane space by transport machineries, such as the TIM chaperone. Currently, the mechanistic and structural details of how the TIM chaperone binds to these mitochondrial proteins remain elusive. To gain structural...

18. Short Talk 9, Annika Söderholm - Structure and substrate specificity of the tryptophan biosynthesis enzyme IGPS from Pseudomonas aeruginosa

Annika Söderholm (Uppsala university)

10/10/2019, 16:30

In bacteria, tryptophan synthesis is performed by the enzymes encoded in the trp operon. The product of the
trpC gene, indole-3-glycerol phosphate synthase (IGPS) catalyzes the indole-forming reaction of tryptophan
synthesis. The reaction mechanism includes a decarboxylation step of the substrate 1-(o-carboxyphenylamino)
1-deoxyribulose 5-phosphate (CdRP). The decarboxylation has been assumed...

19. Keynote 8, Prof. Henning Tidow: Structural studies of integral membrane proteins using stealth carrier nanodiscs

Prof. Henning Tidow (Hamburg University)

10/10/2019, 16:50

Structural studies of integral membrane proteins (IMPs) are challenging, as many of them are inactive or insoluble in the absence of a lipid environment. We pioneered an approach making use of fractionally deuterium labelled ‘stealth carrier’ nanodiscs that are effectively invisible to low-resolution neutron diffraction and enable structural studies of IMPs in a lipidic native-like solution...

17. Keynote 7, Prof. Mei Hong: Structure and Dynamics of Amyloid Proteins from Solid-State NMR: Glucagon & Tau

Prof. Mei Hong (MIT, USA)

Protein misfolding into amyloid fibrils is common not only in neurodegenerative diseases but also in pharmaceutical sciences, where many peptide-based drugs have the tendency to fibrillize, thus impeding solution formulation of the drug. Using solid-state NMR spectroscopy, we have investigated the structure and dynamics of two amyloid fibrils, one formed by the peptide hormone glucagon, which...