121st General Meeting of the KCS

Type Poster Presentation
Area Life Chemistry
Room No. Event Hall
Time 4월 20일 (금요일) 11:00~12:30
Code BIO.P-291
Subject Measurement of hydrogen bonding and conformational change of M2 proton channel using femto-second 2DIR spectroscopy
Authors NAM HYEONG KIM, Yong Ho Kim1,*
Department of Chemistry, Sungkyunkwan University, Korea
1Department of Chemistry, SKKU Advanced Institute of Nano technology, Korea
Abstract The understanding of structural dynamics and the interaction of the transmembrane domain of membrane proteins with the environment is critical to revealing its function mechanism. Among several interactions to construct protein structures, hydrogen bonding interactions are most important for the assembly, structure and function of membrane proteins. In particular, hydrogen bonding between protein and water molecules is of great interest in understanding the role of water molecules in transmembrane protein pores for the transport of substrates across membrane bilayers. Although methods for calculating the structural information of transmembrane domains are advancing, it is still difficult to observe the protein mechanics itself and to measure the interaction with water molecules through hydrogen bonding. Here we use femtosecond two-dimensional infrared spectroscopy to understand the reversible structural changes of the M2 proton channel and the movement of water molecules in the channel protein to understand proton conduction activity. M2 protein of Influenza A virus is one of the smallest proton-selective channels found in nature. This is the ideal system for studying the use of water when selectively transporting protons across the membrane. Stabilization of membrane conditions and enhancement of spectroscopic techniques using a solid support lipid bilayer increase the resolution and intensity of the IR spectrum. The generation of crosspeaks also provides direct information on reversible conformational changes in the transmembrane domain. The results show that 2D IR spectroscopy can provide structural and dynamic information to understand the function of the transmembrane domain.
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