Non-ergodicity of a globular protein extending beyond its functional timescale.

ABSTRACT: Internal motions of folded proteins have been assumed to be ergodic, i.e., that the dynamics of a single protein molecule averaged over a very long time resembles that of an ensemble. Here, by performing single-molecule fluorescence resonance energy transfer (smFRET) experiments and molecular dynamics (MD) simulations of a multi-domain globular protein, cytoplasmic protein-tyrosine phosphatase (SHP2), we demonstrate that the functional inter-domain motion is observationally non-ergodic over the time spans 10^-12 to 10^-7 s and 10^-1 to 10² 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 o

SUBMITTER: Li J 

PROVIDER: S-EPMC9400594 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature