투고논문

Effect of salt on membrane protein Caveolin3 proved with NMR spectroscopy  

Byoungduck Park¹ and Ji-Hun Kim²*

¹ College of Pharmacy, Sahmyook University, Seoul 01795, Republic of Korea

²College of Pharmacy, Chungbuk National University Cheongju, Chungbuk 28160, Republic of Korea

Received Jul 10, 2024; Revised Aug 5, 2024; Accepted Aug 7, 2024

Abstract Caveolin3, mainly expressed in muscle tissue types, is a structural scaffolding protein of caveolae which are microdomains of plasma membrane. To elucidate the relationship between structure and function, several studies on the structure of caveolins using NMR have been reported. Because the ionic strength can affect the electrostatic-driven association of proteins with ligand and protein structure, the effect of salt in the structural studies has to be considered. In this work, we observed that the chemical shifts of Cav3 in the LPPG detergent change depending on salt concentration. The R2 values also show salt concentration-dependent changes. Specifically, in the N-terminal region where conformational changes and various interactions occur, the R2 values decrease. Interestingly, the R2 values of residues expected to be located in the LPPG detergent are also influenced by the salt concentration. This work suggests that the concentration of NaCl can affect interpretation of NMR data from membrane proteins. 

Keywords Caveolin3, NMR, sodium chloride, relaxation, membrane protein

*  Address correspondence to: Ji-Hun Kim, College of Pharmacy, Chungbuk National University, Chengju, Chungbuk 28160, Republic of Korea, Tel: 82-43-249-1343; Fax: 82-43-268-2732; E-mail: nmrjhkim@cbnu.ac.kr