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  • 03월 10일 13시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

대한화학회 제105회 학술발표회 및 총회 Engineering Protein Thermal Stability: Biochemistry, Biophysics, Computation and Bioinformatics

2010년 3월 9일 16시 44분 42초
금13C5심 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
금 11시 : 25분
생명화학 - 단백질 과학의 생화학적 접근
저자 및
서울대학교 농생명공학부, Korea
Engineering proteins for higher thermal stability remains an important but difficult challenge. Clues to designing more stable proteins can be obtained by comparing and contrasting natural proteins from thermophiles, mesophiles and psychrophiles. Three such adenylate kinases were studied to reveal sequential and structural differences responsible for their disparate thermal stabilities. To obtain detailed information about their structures and dynamics, experimental and computational techniques were used. Their crystal structures were solved by X-ray crystallography and their dynamics were studied using molecular dynamics simulations. Based on comparative analysis of the structures and simulations, specific molecular mechanisms for their different thermal stabilities were proposed and tested by in vitro and in silico analysis of mutant enzymes. To further distinguish the roles of specific structural domains in stability and catalysis of adenylate kinase, chimeric enzymes were developed from the thermophilic and mesophilic adenylate kinases. Using a new method with synthetic genes, a series of chimeras were efficiently generated with specific regions exchanged. Analysis of the chimeras revealed that stability and activity were controlled by different domains in adenylate kinase. A bioinformatic method has also been developed to redesign proteins to be more stable through optimization of local structural entropy. The redesigned proteins display significant increases in their thermal stabilities while retaining catalytic activity, and demonstrate a broadly applicable method.