Non-ergodicity of a globular protein extending beyond its functional timescale
Jun Li, Jingfei Xie, Aljaž Godec, Keith Weninger, Cong Liu, Jeremy C. Smith, Liang Hong
Abstract
s. The difference between observational non-ergodicity and simple non-convergence is discussed. In comparison, a single-strand DNA of similar size behaves ergodically with an energy landscape resembling a one-dimensional linear chain. The observed non-ergodicity results from the hierarchical connectivity of the high-dimensional energy landscape of the protein molecule. As the characteristic time for the protein to conduct its dephosphorylation function is ∼10 s, our findings suggest that, due to the non-ergodicity, individual, seemingly identical protein molecules can be dynamically and functionally different.
Topics & Concepts
ErgodicityErgodic theoryGlobular proteinStatistical physicsEnergy landscapePhysicsFörster resonance energy transferMaxima and minimaDomain (mathematical analysis)Chemical physicsBiological systemBiophysicsBiologyMathematicsQuantum mechanicsFluorescencePure mathematicsThermodynamicsNuclear magnetic resonanceMathematical analysisProtein Structure and DynamicsLipid Membrane Structure and BehaviorNanopore and Nanochannel Transport Studies