在α-β平行蛋白折叠过程中,外路物种的大量形成是由于 (非) 原生结构元素在未折叠的分子中对接

Sanne M Nabuurs1, Adrie H Westphal, Carlo P M van Mierlo

  • 1Laboratory of Biochemistry, Wageningen University, Dreijenlaan 3, 6703 HA Wageningen, The Netherlands.

概括

蛋白质的展开揭示了apoflavodoxin中短暂的螺旋结构. 在未折叠状态下,这些非原生相互作用意外地促进了离路径折叠,阻碍了高效的蛋白质折叠.

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