120th General Meeting of the KCS

Type Poster Presentation
Area Life Chemistry
Room No. Exhibition Hall 2+3
Time 10월 19일 (목요일) 11:00~12:30
Code BIO.P-280
Subject NMR dynamics study of SP-isoform from Zoarces elongates Kner
Authors Seo-Ree Choi, Joon-Hwa Lee*, Ae-Ree Lee, Yeo-Jin Seo
Department of Chemistry, Gyeongsang National University, Korea
Abstract Antifreeze proteins (AFPs) are found in a variety of cold-adapted (psychrophilic) organisms to promote survival at subzero temperatures by binding to ice crystals and decreasing the freezing temperature of body fluids. One of most widely studied classes of AFPs is the type III from arctic fish such as the ocean pout and Japanese notched-fin eel pout. The type III AFPs are small globular proteins that consist of one α-helix, three 310-helices, and two β-strands. The type III AFPs have been categorized into two subgroups, quaternary-amino-ethyl (QAE) and sulfopropyl-Sephadex-binding (SP), based on differences in their isoelectric points. The QAE isoforms is able to halt the growth of ice, whereas the SP isoforms are unable to stop the growth of ice crystals. In this study, we have investigated backbone dynamics analyses of two kinds of type III AFPs from Japanese notched-fin eel pout (Zoarces elongates Kner), nfeAFP6 (SP), nfeAFP6_tri at various temperatures. We also characterized the structural/dynamic properties of the ice-binding surfaces by analyzing the temperature gradient of the amide proton chemical shift and its correlation with chemical shift deviation from random coil. This study provides insight into the molecular basis of ice-binding and antifreezing activities of type III AFP isoforms.
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