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  • 09월 01일 18시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제118회 대한화학회 학술발표회, 총회 및 기기전시회 안내 NMR study of type III antifreeze protein from Zoarces elongates Kner

2016년 8월 30일 11시 10분 41초
BIO.P-151 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 14일 (금요일) 11:00~12:30
저자 및
최서리, 이애리, 이준화*
경상대학교 화학과, Korea
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 proteins can be further divided into two subgroups, QAE1 and QAE2. QAE2 isoforms can slow, but not stop, the growth of ice crystals by binding to pyramidal ice planes. The other group (QAE1) binds both pyramidal and primary prism planes and is able to halt the growth of ice. In this study, we have investigated backbone dynamics analyses of four kinds of type III AFPs from Japanese notched-fin eel pout (Zoarces elongates Kner), wt AFP8 (QAE1), V20A_AFP8 , V20G_AFP8, AFP8_di and AFP8_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