Conformations and folding of lysozyme ions in vacuo
Conformations and folding of lysozyme ions in vacuo
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DOI：
10.1073/pnas.93.7.3143
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发表时间：
1996-04-02
影响因子：
11.1
通讯作者：
Williams, ER
中科院分区：
文献类型：
--
作者：
Gross, DS;Schnier, PD;Williams, ER
蛋白质鸡蛋清溶菌酶的分离电荷态的质子转移反应性表明，该蛋白质的多种不同构象在气相中是稳定的。（二硫化物-完整）和“变性"（二硫化物还原）溶液，分别与其晶体结构和完全变性构象中离子的计算值一致，低于8+的两种形式，由质子剥离形成的电荷状态，具有相似或难以区分的反应性，表明二硫化物还原的离子在气相中折叠成更紧凑的构象。
Proton transfer reactivity of isolated charge states of the protein hen egg-white lysozyme shows that multiple distinct conformations of this protein are stable in the gas phase, The reactivities of the 9+ and 10+ charge state ions, formed by electrospray ionization of ''native'' (disulfide-intact) and ''denatured'' (disulfide-reduced) solutions, are consistent with values calculated for ions in their crystal structure and fully denatured conformations, respectively, Charge states below 8+ of both forms, formed by proton stripping, have similar or indistinguishable reactivities, indicating that the disulfide-reduced ions fold in the gas phase to a more compact conformation.