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제109회 대한화학회 학술발표회, 총회 및 기기전시회 안내 Impact of Surface Chemical Heterogeneity on Protein Self-Assembly in Water

2012년 2월 10일 17시 13분 05초
PHYS.P-286 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
4월 25일 (수요일) 18:00~21:00
저자 및
정성호, 함시현
숙명여자대학교 화학과, Korea
Hydrophobicity is thought to underlie self-assembly in biological systems. However, the protein surface comprises hydrophobic and hydrophilic patches, and understanding the impact of such a chemical heterogeneity on the protein self-assembly in water is of fundamental interest. Here, we report structural and thermodynamic investigations on the dimer formation of amyloid-beta proteins in water using the unguided, fully atomistic, explicit-water molecular-dynamics simulations as well as the integral-equation theory of liquids. We demonstrate a key role of hydrophilic residues in initiating the dimerization process: a long-range water-mediated attractive force of enthalpic origin acting on the hydrophilic residues provides the major thermodynamic force that drives two proteins to approach from a large separation to a contact distance. After two proteins make atomic contacts, the nature of the water-mediated attraction changes from a long-range enthalpic interaction to a short-range entropic one. The latter acts both on the hydrophobic and hydrophilic residues. Along with the direct protein-protein interactions that lead to the formation of inter-monomer hydrogen bonds and van der Waals contacts, the water-mediated attraction of entropic origin induces structural adjustment of constituent monomer proteins toward the formation of a compact dimer structure.