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Solid-state NMR studies of proteins in condensed phases

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摘要 Some proteins perform their biological functions by changing their material states through liquid-liquid phase separation.Upon phase separation,the protein condenses into a concentrated liquid phase and sometimes into a gel phase,changing its dynamic properties and intermolecular interactions,thereby regulating cellular functions.Although the biological significance of this phenomenon has been widely recognized by researchers,there is still a lack of a comprehensive understanding of the structural and dynamic properties of the protein in the condensed phase.In this phase,molecules usually contain domains with varied dynamic properties and undergo intermediate exchanges.Magic angle spinning(MAS)solid-state NMR(SSNMR)experiments are very powerful in studying rigid protein polymers such as amyloid.The incorporation of solution-like experiments into SSNMR and the development of J-coupling based MAS SSNMR techniques extend its ability to study partially mobile segments of proteins in a condensed liquid or gel phase which are not visible by solution NMR or dipolar-coupling based SSNMR.Therefore,it has been applied in studying protein condensation and has provided very important information that is hard to obtain by other techniques.
出处 《Magnetic Resonance Letters》 2024年第3期1-10,共10页 磁共振快报(英文)
基金 supported by the National Natural Science Foundation of China(No.32171185,No.31770790) the National Key R&D Program of China(No.2017YFA0504804).
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