Probing Adaptation of Hydration and Protein Dynamics to Temperature

Abstract

Protein dynamics is strongly influenced by the surrounding environment and physiological conditions. Here we employ broadband megahertz-to-terahertz spectroscopy to explore the dynamics of water and myoglobin protein on an extended time scale from femto- to nanosecond. The dielectric spectra reveal several relaxations corresponding to the orientational polarization mechanism, including the dynamics of loosely bound, tightly bound, and bulk water, as well as collective vibrational modes of protein in an aqueous environment. The dynamics of loosely bound and bulk water follow non-Arrhenius behavior; however, the dynamics of water molecules in the tightly bound layer obeys the Arrhenius-type relation. Combining molecular simulations and effective-medium approximation, we have determined the number of water molecules in the tightly bound hydration layer and studied the dynamics of protein as a function of temperature. The results provide the important impact of water on the biochemical functions of proteins.

Dynamics of Hydrogen Bonds between Water and Intrinsically Disordered and Structured Regions of Proteins

“…Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of otherwise structured proteins are ubiquitous and involved in many signaling and regulatory processes. − Interactions between proteins and water and the dynamics of water around proteins play key roles in protein function, including enzyme activity and allostery, , and while these properties have been extensively studied for structured proteins, − less is known for IDPs and proteins with IDRs. Some studies indicate more restricted dynamics of water around IDRs and IDPs compared to structured systems of similar size, − the origin of which appears to be due at least in large part to a greater presence of charged groups in disordered regions .…”

Plant root associated chitinases: structures and functions

“…Oryza sativa normally grows emerged in water ( Yan et al., 2023 ), whereas Zea mays grows under more dry conditions on land. Differences in the charge distributions of Zm Chi19A and Os Chi19A may be adaptations to specific ecological niches, lifestyles, or host-pathogen interactions ( Vanhoye et al., 2004 ; Garcia-Moreno, 2009 ; Gerland et al., 2020 ; Kim et al., 2020 ; Panja et al., 2020 ; Di Savino et al., 2021 ; Doan et al., 2022 ; Vallina Estrada et al., 2023 ).…”