Advanced Research on Structure-Function Relationships of Membrane Proteins, 2nd Edition

Recent developments in the methodology of structure determination provide high-resolution structures of membrane proteins, and a number of high-resolution structures of membrane proteins have been reported (3.9% of PDB in 2026). Solid-state NMR spectroscopy does not require crystallization and is not restricted by the upper limits to molecular weight. Solution NMR spectroscopy is recently used to determine structure of membrane proteins by using nanodisc as a membrane mimic system. For X-ray crystallography, it is becoming possible to determine structures of membrane proteins by using membrane or membrane mimic systems to form the crystals. The recently developed time-resolved method allows determining the structure of short-lived intermediates of membrane proteins. Attention is now being focused on cryo-electron microscopy as a powerful method to determine the structure of membrane proteins using two-dimensional crystals. The determination of membrane protein structure based on single-molecular observation has become possible.

This Special Issue focuses on advanced studies on structure-function relationships using advanced methods to determine the high-resolution structure of membrane proteins, including developments in methodology. Within the scope of this Special Issue are not only the determination of a complete structure but also of local structure changes and dynamic properties of membrane proteins.