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Native hydrogen bonds in a molten globule: The apoflavodoxin thermalintermediate

机译:熔融小球中的天然氢键:载脂蛋白毒素热中间体

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The structure and energetics of protein-folding intermediates are poorly understood. We have identified, in the thermal unfolding of the apoflavodoxin from Anabaena PCC 7119, an equilibrium intermediate with spectroscopic properties of a molten globule and substantial enthalpy and heat capacity of unfolding. The structure of the intermediate is probed by mutagenesis land phi analysis) of polar residues involved in surface-exposed hydrogen bonds connecting secondary-structure elements in the native protein. All hydrogen bonds analysed are formed in the molten globule intermediate, either with native strength or debilitated. This suggests the overall intermediate's topology and surface tertiary interactions are close to native, and indicates that hydrogen bonding may contribute significantly to shape the conformation and energetics of folding intermediates.
机译:人们对蛋白质折叠中间体的结构和能量学知之甚少。我们已经从鱼腥藻PCC 7119的载脂黄素毒素的热展开中发现了一种平衡中间体,该中间体具有熔融小球的光谱特性,并且具有相当大的焓和展开的热容量。中间体的结构通过诱变陆地化学分析来探测,该极性残基涉及与天然蛋白质中二级结构元素相连的表面暴露氢键。所分析的所有氢键均在熔融小球中间体中形成,或者具有天然强度,或者具有衰弱性。这表明整个中间体的拓扑结构和表面三级相互作用都非常接近于天然,并表明氢键可显着影响折叠中间体的构象和能量。

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