2022 article
Non-ergodicity of a globular protein extending beyond its functional timescale
Li, J., Xie, J. F., Godec, A., Weninger, K. R., Liu, C., Smith, J. C., & Hong, L. (2022, August 4). CHEMICAL SCIENCE.
TL;DR:
By performing single-molecule fluorescence resonance energy transfer experiments and molecular dynamics simulations of a multi-domain globular protein, cytoplasmic protein-tyrosine phosphatase (SHP2), it is demonstrated 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.
(via Semantic Scholar)
open access via pubs.rsc.org (publisher PDF)
UN Sustainable Development Goal Categories
3. Good Health and Well-being
(Web of Science)
7. Affordable and Clean Energy
(OpenAlex)
Source: Web Of Science
Added: August 22, 2022
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.