The first proposal of the origins of the catalytic power of enzymes came almost 100 years ago, when Haldane posited that enzymes stabilize the transition state of the catalyzed reaction, thus accelerating the chemical transformation step [1]. Detailed structural studies indeed showed that enzymes have specific regions where catalysis occurs, appropriately called them ‘active sites’. However, the static picture of macromolecular objects fails to explain the origins of the catalytic power, and it has long been recognized that motions in proteins are essential for their biological roles [2, 3, 4]. Of course, molecules at 300K cannot be static objects but, as Hans Frauenfelder asserted, the point is to distinguish the functionally important motions (FIMs) from the biologically unimportant motions (BUMs) [5,6]. The FIMs may facilitate substrate binding and alignment in the reaction center, barrier crossing, product release, etc, and they must underlie the secrets of allostery, the necessary condition that protein activity must be physiologically adjustable by external regulators.