Abstract
A large portion of proteins in living organisms are membrane proteins which play critical roles in the biology of the cell, from maintenance of the biological membrane integrity to communication of cells with their surroundings. To understand their mechanism of action, structural information is essential. Nevertheless, structure determination of transmembrane proteins is still a challenging area, even though recently the number of deposited structures of membrane proteins in the PDB has rapidly increased thanks to the efforts using X-ray crystallography, electron microscopy, and solid and solution nuclear magnetic resonance (NMR) technology. Among these technologies, solution NMR is a powerful tool for studying protein-protein, protein-ligand interactions and protein dynamics at a wide range of time scales as well as structure determination of membrane proteins. This review provides general and useful guideline for membrane protein sample preparation and the choice of membrane-mimetic media, which are the key step for successful structural analysis. Furthermore, this review provides an opportunity to look at recent applications of solution NMR to structural studies on α-helical membrane proteins through some success stories.
Highlights
Membrane proteins (MPs) represent ~30% of all proteins in living organisms [1]
Molecules 2017, 22, 1347 structures still represent less than 2% of the total number of structures; this state of affairs means that determination of MP structure remains a challenge at present
This review will briefly provide guidelines on what needs to be done to determine the MP structure by solution nuclear magnetic resonance (NMR) analysis, and discuss some details on membrane-mimetic media according to the analysis of the structures deposited in Protein Data Bank (PDB)
Summary
Membrane proteins (MPs) represent ~30% of all proteins in living organisms [1]. They play many important roles in a wide range of cellular functions such as transport, transmission of cell signaling and scaffold support [2]. When compared with X-ray crystallography and EM, NMR can provide unique and interesting information such as protein dynamics on a wide range of time scales and interactions with internal or other components in the membrane-associated region, generally regarded as the “blind spot” in structural biology; these data offer a chance to understand the biological roles of MP [19]. All these information can be detected at the individual amino acid level (e.g., via recording intensity or chemical shift values) and are directly related to quality of the NMR spectra. This review will briefly provide guidelines on what needs to be done to determine the MP structure by solution NMR analysis, and discuss some details on membrane-mimetic media according to the analysis of the structures deposited in PDB
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