Slow Protein Conformational Change, Allostery and Network Dynamics

Allosteric Activation Transitions in Enzymes and Biomolecular Motors: Insights from Atomistic and Coarse-Grained Simulations

“…It is tempting to ask how do the dynamic properties of proteins/enzyme fit in the broader biological context, such as protein-protein interaction networks in the cell and protein evolution. For example, interesting discussions have been made regarding slow protein conformational fluctuations (i.e., dynamic disorder of protein activity) as an additional origin of stochasticity for protein interaction network 111 ; therefore, the time-scale of slow protein fluctuations might need to be tuned in the cellular context to be compatible with the sensitivity and robustness of the underlying protein network. Along this line, it is increasingly realized that the cellular environment is very different and effects such as molecular crowding has a major impact on the binding and dynamic properties as well as the stability of biomolecules 112 .…”

Functional Roles of Slow Enzyme Conformational Changes in Network Dynamics

“…In cell biology this phenomenon of dynamic disorder is usually called ''nongenetic heterogeneity'' (50). When the corresponding deterministic dynamics of a network is near a transition point, e.g., a bifurcation point, consequences of the transient parameter fluctuations can be further amplified and temporarily frozen (51,52), as illustrated in Fig. 4 e, which may explain the observed larger and slower timescale (in days or longer) stochasticity (53).…”