From structural biology to enzyme design or optimized pharmacology, modulation of the thermal stability of proteins can be accurately modeled with our technology.
A recent example was published in the Journal of Chemical Theory and Computation:
QresFEP: an automated protocol for free energy calculations of protein mutations in Q
W. Jespers, G.V. Isaksen, T.A.H. Andberg, S. Vasile, A. van Veen, J. Åqvist, B.O. Brandsdal, H. Gutiérrez-de-Terán, Journal of Chemical Theory and Computation 2019, 15 (10), 5461–5473.
Calculations of the relative stability of T4-lysozyme due to single point mutations. (A) Thermodynamic cycle used, where the folded-state is on the top horizontal leg with mutated positions represented in orange sticks. The unfolded state (bottom leg) is represented by a simple Ala-X-Ala tripeptide. (B) Experimental versus calculated shifts in thermal stability, expressed as ΔΔG (Kcal/mol), for the 43 mutants as calculated with QresFEP (blue dots) and FEP+ (orange dots). The solid line represents a perfect correlation, and the dotted and dashed lines indicate the thresholds at ±1 and ±2 kcal/mol respectively
