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Computational Study on the Inversion of Possible Secondary Structures of the β-Peptides

등록일
2009년 8월 14일 15시 27분 02초
접수번호
1189
발표코드
34P217포 이곳을 클릭하시면 발표코드에 대한 설명을 보실 수 있습니다.
발표시간
목 <발표Ⅰ>
발표형식
포스터
발표분야
물리화학
저자 및
공동저자
이주희, 함시현
숙명여자대학교 화학과, Korea
Interest in β-peptides has recently turned towards the residue-based control of secondary structure formation, and it was proved that the stereochemistry effects on the β-peptides folding. β-peptides composed of trans-2-aminocyclohexanecarboxylic acid (trans-ACHC) and trans-2-cyclopentanecarboxylic acid (trans-ACPC) had been reported to exhibit a high propensity to form helical structures. Unlike that, β-peptides composed of cis-2-cyclopentanecarboxylic acid (cis-ACPC) were assigned to be strand structures by using the NMR spectroscopy. In this study, the homo-oligomers composed of (1R,2R)-trans-ACPC and (1R,2S)-cis-ACPC as model systems were employed to examine the effects of the stereochemistry for the stability of β-peptides. Here, we performed the conformational annealing method by using molecular dynamics simulation and selected model ACPC conformers were optimized by the density functional theory to evaluate briefly the conformational preference and the thermodynamic properties such as relative stability, dipole moment, free energy, enthalpy, and entropy of the model systems. The results of these theoretical approaches would give the structural propensities and thermodynamic stabilities of the secondary structures in the β-peptides.

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