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제124회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Free Energy Landscape of Coupled Folding and Binding

2019년 8월 15일 22시 40분 54초
PHYS.P-135 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
10월 17일 (목요일) 11:00~12:30
Physical Chemistry
저자 및
Song-Ho Chong, Haeri Im, Sihyun Ham*
Department of Chemistry, Sookmyung Women's University, Korea
The most fundamental aspect of the free energy landscape of proteins is that it is globally funneled such that protein folding is energetically biased. Then, what are the distinctive characteristics of the landscape of intrinsically disordered proteins, apparently lacking such energetic bias, that nevertheless fold upon binding? Here, we address this fundamental issue through the explicit characterization of the free energy landscape of the paradigmatic pKID–KIX system. This is done based on unguided, fully atomistic, explicit-water molecular dynamics simulations with an aggregated simulation time of >30 microseconds and on the computation of the free energy that defines the landscape. We find that, while the landscape of pKID before binding is considerably shallower than the one for a protein that autonomously folds, it gets progressively more funneled as the binding of pKID with KIX proceeds. This explains why pKID is disordered in a free state, and the binding of pKID with KIX is a prerequisite for pKID’s folding. In addition, we observe that the key event in completing the pKID–KIX coupled folding and binding is the directed self-assembly where pKID is docked upon the KIX surface to maximize the surface electrostatic complementarity, which, in turn, require pKID to adopt the correct folded structure. This key process shows up as the free energy barrier in the pKID landscape separating the intermediate nonspecific complex state and the specific complex state. The present work not only provides a detailed molecular picture of the coupled folding and binding of pKID, but also expands the funneled landscape perspective to intrinsically disordered proteins.