Reynolds J A
J Biol Chem. 1976 Oct 10;251(19):6013-5.
An investigation of the denaturation of the major polypeptides from human serum high density lipoprotein by guanidine hydrochloride reveals that the lipid-free, water-soluble states are minimally stable relative to the random coil states. These findings are in direct contrast to the resistance of intrinsic membrane proteins (in the absence of ligand) to complete unfolding by the same denaturant. Consideration of the denaturation data for the apolipoproteins together with previously published data from this laboratory on ligand-induced conformational changes indicate that these polypeptides possess several similar conformational states which are readily interconvertible.
一项关于盐酸胍对人血清高密度脂蛋白主要多肽变性作用的研究表明，相对于无规卷曲状态，无脂质的水溶性状态稳定性最低。这些发现与内在膜蛋白（在无配体情况下）对相同变性剂完全展开的抗性形成直接对比。结合载脂蛋白的变性数据以及本实验室先前发表的关于配体诱导构象变化的数据进行考虑，表明这些多肽具有几种易于相互转化的相似构象状态。
