溶菌酶
折叠(DSP实现)
蛋白质二级结构
化学
圆二色性
二硫键
蛋白质折叠
结晶学
蛋白质二硫键异构酶
胞壁酶
生物化学
电气工程
工程类
作者
Michel Goldberg,Yvonne Guillou
标识
DOI:10.1002/pro.5560030603
摘要
Abstract To assess the respective roles of local and long‐range interactions during protein folding, the influence of the native disulfide bonds on the early formation of secondary structure was investigated using continuous‐flow circular dichroism. Within the first 4 ms of folding, lysozyme with intact disulfide bonds already had a far‐UV CD spectrum reflecting large amounts of secondary structure. Conversely, reduced lysozyme remained essentially unfolded at this early folding time. Thus, native disulfide bonds not only stabilize the final conformation of lysozyme but also provide, in early folding intermediates, the necessary stabilization that favors the formation of secondary structure.
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