Protein dynamics as a stabilizing force

Prof. Kaare Teilum (University of Copenhagen, Denmark)

Thursday, 25 September 2025

16:00

Johannes Kepler University Linz

Room: KG 519

Using an E. coli based in-cell stability assay we have selected a super-stabilized variant of chymotrypsin inhibitor 2 (CI2) carrying two point mutations. This double mutant is significantly more stable than the sum of the effects of the two individual single point mutations.

To understand the underlying mechanism for this synergistic effect we have made a thorough analysis of the structural and dynamical changes occurring as a result of the mutations. NMR relaxation measurements show that the stability change correlate with the change in conformational entropy.

Our results demonstrate that changes in dynamics distributed throughout the protein are hard to predict but may contribute significantly to protein stability.