Kinetic extreme stability

I was recently attracted by a paper in PNAS, "Designed protein reveals structural determinants of extreme kinetics stability", see paper here. Generally, when thinking to protein stability my first vision relates to the stability curve measuring the free energy difference between the folded and unfolded states as it changes with temperature. This is stability in thermodynamic sense. And this means, for example, in a probabilistic perspective, how many folded proteins are found at a given thermodynamic condition in a solution, and assuming that all the possible states (folded and unfolded) are sampled. But, one protein can survive in its folded state just because the barrier separating it to the unfolded floppy configuration is too high. This is the case for example for the protein a-lytic protease, that is really kinetically stable although the unfolded state is lower in energy. The authors, by de nove design constructed a protein which is at once thermodynamically and kinetically stable. The protein is named ThreeFoil and is a repeat of three peptide domains with both alpha and beta secondary structures. The interesting part of the paper is the correlation found among the extreme kinetic stability and  some metrics describing the relative contacts between the amino-acids in the structure (absolute contact order, ACO, and long-range order, LRO) which in turn account for the possibility to have unfolding event highly cooperative.

From the article in PNAS (PNAS 2015 112 (47) 14605-14610)