HOW RANDOM IS A HIGHLY DENATURED PROTEIN
HOW RANDOM IS A HIGHLY DENATURED PROTEIN
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DOI：
10.1016/0301-4622(94)00081-6
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发表时间：
1994-12-01
影响因子：
3.8
通讯作者：
SMITH, JC
中科院分区：
文献类型：
--
作者：
CALMETTES, P;DURAND, D;SMITH, JC
人们对确定蛋白质变性状态的物理化学性质重新产生了兴趣。在许多变性态中，有证据表明非随机构型分布的存在。在这里，我们研究了酵母磷酸甘油激酶在天然状态和高度变性条件下的小角中子散射谱。我们表明，变性蛋白质的散射曲线可以用合成聚合物的模型来解释，其中链在良好的溶剂中表现为随机线圈，即排除了体积相互作用。讨论了这一结果对我们了解蛋白质折叠过程的意义。
There has been renewed interest in determining the physicochemical properties of denatured states of proteins. In many denatured states there is evidence for the existence of nonrandom configurational distributions. Here we examine the small-angle neutron scattering profile of yeast phosphoglycerate kinase in the native state and in highly denaturing conditions. We show that the denatured protein scattering profile can be interpreted using a model developed for synthetic polymers in which the chain behaves as a random coil in a good solvent, i.e. with excluded volume interactions. The implications of this result for our appreciation of the protein folding process are discussed.