화학공학소재연구정보센터
학회 한국화학공학회
학술대회 2002년 봄 (04/26 ~ 04/27, 강원대학교)
권호 8권 1호, p.1245
발표분야 생물화공
제목 단백질 3차 구조를 구성하는 아미노산의 구조적 성질들의 분자 수준 해석과 통계적 해 석
초록 Molecular calculations, and statistical analyses, were performed to investigate the
relationships between residual conformational properties of amino acid as building blocks
in three-dimensional protein structures. 100 monomeric protein structures were employed
as representative model systems. In each protein, various residual conformational
properties, such as; exposure ratio, packing value, surface area, solvation free energy,
residual energy, flexibility, secondary structure, and several stabilizing interactions, were
calculated. After each residual property of all the model proteins were statistically
analyzed, distinct and similar patterns were obtained according to the amino acid type.
For arranging several residual conformational properties, the dendrogram describing the
conformational relationship among 20 amino acids in a protein structure was proposed
via hierarchical cluster analysis. The results of the residual conformational property
patterns, and clusters among the amino acids, could serve as basic data for analyzing
local protein structure, and for predicting local protein function.
저자 백승필, 최유성, 민경선, 유영제
소속 서울대
키워드 Residual conformational property; Statistical analysis; Protein structure
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