Journal
MEMBRANES
Volume 11, Issue 8, Pages -Publisher
MDPI
DOI: 10.3390/membranes11080604
Keywords
membrane protein; NMR; ion channel; GPCR; transporter; dynamics
Categories
Funding
- Japan Agency forMedical Research and Development Grant [JP18ae010104]
- Japan Society for the Promotion of Science, KAKENHI [JP17H06097, JP20H04722, JP20H03378, JP20K21494]
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Multi-spanning membrane proteins transfer information and materials through a membrane by changing their conformations, and their dynamics are closely related to their function. NMR reveals dynamics information that can discriminate function-related dynamics from random fluctuations. Studies using solution NMR have contributed to revealing the structural basis of the function of multi-spanning membrane proteins.
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.
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