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  • 09월 20일 16시 이후 : 초록수정 불가능, 일정확인 및 검색만 가능

제126회 대한화학회 학술발표회 및 총회 Unveiling Terminal Residue-Dependent Electrostatic Interactions in Circularly Permuted and Split Outer Membrane Protein

2020년 9월 17일 15시 26분 27초
LIFE.P-310 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 21일(수) 17:30~18:00
Life Chemistry
저자 및
Jaewon Lee, Woon Ju Song1,*
Chemistry, Seoul National University, Korea
1Department of Chemistry, Seoul National University, Korea
Outer membrane protein (Omp) has a critical role in small molecule and protein translocation, as well as signal transduction. The Omp folding into the outer membrane of gram-negative bacteria have been well known to be assisted by β-barrel assembly machinery complex. However, the chemical mechanisms of spontaneous folding into outer membrane have not yet been elucidated. Here, we carried out circular permutation, split and complementation, and point mutation of outer-membrane protein F (OmpF), one of the most abundant and functional β-barrel proteins in gram-negative bacteria. By altering the terminal residues, which expected to interact with lipid head group during folding into membrane, we demonstrate that the terminal residues affect the folding efficiency and kinetics of circularly permuted OmpF. Our results suggest that the folding of the native β-barrel integral membrane proteins is tightly controlled, downregulating non-enzymatic and spontaneous folding process. In addition, our work provides unprecedented strategy for improving folding efficiency of β-barrel membrane protein in various applications.