Abstract
A primary biological function of multi-spanning membrane proteins is to transfer information and/or materials through a membrane by changing their conformations. Therefore, particular dynamics of the membrane proteins are tightly associated with their function. The semi-atomic resolution dynamics information revealed by NMR is able to discriminate function-related dynamics from random fluctuations. This review will discuss several studies in which quantitative dynamics information by solution NMR has contributed to revealing the structural basis of the function of multi-spanning membrane proteins, such as ion channels, GPCRs, and transporters.
Highlights
Multi-spanning helical membrane proteins, such as G-Protein Coupled Receptors (GPCRs), ion channels, and transporters, play a critical role in transferring information and materials through a membrane
Membrane proteins are under conformational equilibrium between different conformational states that are tightly associated with distinctive functional states
The exchange rates between the distinct conformational states described by NMR can define the time scale of the cell response as exemplified for ion channels and GPCRs
Summary
Multi-spanning helical membrane proteins, such as GPCRs, ion channels, and transporters, play a critical role in transferring information and materials through a membrane. Membranes 2021, 11, 604 open state defines the total ion flux, the activity of the ion channel can be described from the stochastic dynamic behavior of the proteins and is beyond the description by static snapshot structures. NMR is able to define the function-associated dynamics in a site-specific manner and quantify the population of each conformation under an equilibrium, along with the rate of interconversion. Due to its versatility to the condition, NMR can monitor the changes in structure and dynamics of membrane proteins associated with the functionally important parameters such as temperature, pH, ions, and inducers. We will overview some recent achievements that highlight the strength of solution-state NMR in the structure and dynamics analyses of the multi-spanning helical membrane proteins, such as ion channels, GPCRs, and transporters
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