Dispersed OmpT may be partially folded
作者单位：College of Chemistry and Molecular Engineering and Biodynamic Optical Imaging Center（BIOPIC）Peking University
会议名称：《中国化学会-生物物理化学专业委员会第四届全国生物物理化...》
会议日期：2016年
学科分类：0710[理学-生物学] 071010[理学-生物化学与分子生物学] 07[理学]
关 键 词：OmpT smFRET urea denaturation partial folding
摘 要：It is believed that outer membrane proteins in Gram-negative bacteria are protected by chaporones during their translocation through the periplasm because they are structureless and prone to aggregation. The previous work on OmpC supported such an opinion. However, recently we found that OmpT has less tendency to aggregate and may be partially folded in its dispersed form. By using single molecule fluorescence resonance energy transfer（smFRET）, the equilibrium denaturation of OmpT induced by urea has been investigated. Double-cysteine mutant（S1C/F297C） of OmpT is engineered and labeled with FRET dyes. We observed subpopulations of denatured and partially folded form of OmpT and the two subpopulations show two-state transition as urea concentration changes. These resluts may help better understanding of outer membrane protein folding.