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Slowdown of Water Dynamics from the Top to the Bottom of the GroEL Cavity

Nicolas Macro, Long Chen, Yushan Yang, Tridib Mondal, Lijuan Wang, Amnon Horovitz, Dongping Zhong

2021The Journal of Physical Chemistry Letters14 citationsDOIOpen Access PDF

Abstract

The GroE molecular chaperone system is a critical protein machine that assists the folding of substrate proteins in its cavity. Water in the cavity is suspected to play a role in substrate protein folding, but the mechanism is currently unknown. Herein, we report measurements of water dynamics in the equatorial and apical domains of the GroEL cavity in the apo and football states, using site-specific tryptophanyl mutagenesis as an intrinsic optical probe with femtosecond resolution combined with molecular dynamics simulations. We observed clearly different water dynamics in the two domains with a slowdown of the cavity water from the apical to equatorial region in the football state. The results suggest that the GroEL cavity provides a unique water environment that may facilitate substrate protein folding.

Topics & Concepts

GroELFolding (DSP implementation)Chaperone (clinical)BiophysicsProtein foldingChemical physicsMolecular dynamicsChaperoninSubstrate (aquarium)SlowdownChemistryCrystallographyNanotechnologyBiologyMaterials scienceBiochemistryEcologyComputational chemistryPolitical scienceGeneLawEngineeringEscherichia coliPathologyMedicineElectrical engineeringProtein Structure and DynamicsHeat shock proteins researchEnzyme Structure and Function
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