| 학회 |
한국화학공학회 |
| 학술대회 |
2003년 봄 (04/25 ~ 04/26, 순천대학교) |
| 권호 |
9권 1호, p.456 |
| 발표분야 |
생물화공 |
| 제목 |
Folding characteristics of small globular proteins: equilibrium sampling and structural analysis by molecular simulations |
| 초록 |
The structural distribution along folding pathways is characterized by the equilibrium sampling of protein structures in which effective energy functions are coupled to topological energies. For the efficient sampling of protein structures, temperature replica exchange method is employed here where 8 replicas are used with temperatures distributed exponentially and structural analysis is performed by weighted histogram method. Free energy profiles plotted along nativeness order parameter clearly show the existence of two wells, denatured and native states, as well as transition state (TS) analog. From structural folding pathways, conformations within TS analog are obtained, which are in harmony with experimental data. Moreover, through reduced model simulations, it is found that the hydrophobicity among sequence-dependant interactions is a critical role to determine the lowest free energy pathway among many possible folding routes of protein G. |
| 저자 |
이승엽1, Yoshimi Fujitsuka2, Shoji Takada2, 김도현1
|
| 소속 |
1KAIST 생명화학공학과 & 초미세화학공정시스템연구센터, 2고베대 |
| 키워드 |
protein folding; molecular simulation; equilibrium sampling; coarse grained model; pi value analysis
|
| E-Mail |
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| VOD |
VOD 보기 |
