CAJ | 학술논문

圆二色谱仪是研究蛋白质二级结构的有力工具,能在远紫外区测出蛋白质的二级结构的各种构象.通常的蛋白质二级结构有α-螺旋、β-折叠、反β-折叠、β-转角及无规则卷曲五种构象,实际观测到的CD谱是这几种二级结构构象CD谱的线性加和.本文利用了奇异值分解最小二乘算法(SVDLS),并编译相关程序解析现场外加电压电解条件下的蛋白质溶液的CD谱,得到几种二级结构构象的组分分布.所得结果与文献报道上的其他方法如SELCON3等相比较,证明是一种快速和有效的方法.
원이색보의시연구단백질이급결구적유력공구,능재원자외구측출단백질적이급결구적각충구상.통상적단백질이급결구유α-라선、β-절첩、반β-절첩、β-전각급무규칙권곡오충구상,실제관측도적CD보시저궤충이급결구구상CD보적선성가화.본문이용료기이치분해최소이승산법(SVDLS),병편역상관정서해석현장외가전압전해조건하적단백질용액적CD보,득도궤충이급결구구상적조분분포.소득결과여문헌보도상적기타방법여SELCON3등상비교,증명시일충쾌속화유효적방법.
The circular dichroism spectrometer is an excellent tool for the study of the secondary structure of proteins in so-lution, since every kinds of protein have their apparent CD band in UV region. Generally, a common protein with secondarystructure includes five conformations, α-helix, β-sheet, anti-β-sheet, β-turn and random coil. The experimental CD spec-tra of the protein are the linear combination of each CD spectrum of the five conformations '. We used the mathematicalmethod of singular value decomposition and least squares (SVDLS) to compile a computer program to solve the in-situ CDspectra of protein under the applied potentials, and got the fraction distribution curves of the five conformation changes. Theresults obtained were compared with the ones obtained from other programs reported before, such as SELCON3, which indi-cates that our program is a quick and effective method to solve this problem.