UNUSUALLY STABLE HELIX FORMATION IN SHORT ALANINE-BASED PEPTIDES
UNUSUALLY STABLE HELIX FORMATION IN SHORT ALANINE-BASED PEPTIDES
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DOI：
10.1073/pnas.86.14.5286
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发表时间：
1989-07-01
影响因子：
11.1
通讯作者：
BALDWIN, RL
中科院分区：
文献类型：
--
作者：
MARQUSEE, S;ROBBINS, VH;BALDWIN, RL
短的、16-残基的、基于丙氨酸的肽显示稳定的α-在水中形成螺旋。当与关于α-β的经典观点对比时，该结果是令人惊讶的。螺旋作为一个边缘稳定的结构在水和认为短螺旋不稳定。丙氨酸基肽通过插入三个或更多个单电荷类型的残基赖氨酸（+）或谷氨酸（-）而溶解。结果不能解释由浓度依赖性协会或由带电残基与螺旋偶极子的相互作用产生的螺旋稳定。我们的结果不是由“主-客”方法确定的丙氨酸和赖氨酸的参数预测的：这些参数预测16-残基肽不应显示可测量的α-氨基酸。螺旋形成疏水相互作用在α-β-环糊精中的作用分析螺旋形成[理查兹，F. M.和里士满，T.（1978）在Molecular Interactions and Activity in Proteins，Ciba Foundation Symposium 60，ed. Wolstenholme，G. E.（Excepta Medica Amsterdam），pp. 23-25]在丙氨酸残基的螺旋嵌段中没有显示出异常强的疏水相互作用。因此，对我们结果的可能解释是，单个丙氨酸残基具有高螺旋势。目前还不知道是否有其他氨基酸显示出这种特性，这种特性的起源也是未知的。
Short, 16-residue, alanine-based peptides show stable .alpha.-helix formation in H2O. This result is surprising when contrasted with the classical view that regards the .alpha.-helix as a marginally stable structure in H2O and considers short helices unstable. The alanine-based peptides are solubilized by insertion of three or more residues of a single charge type, lysine (+) or glutamic acid (-). The results cannot be explained by helix stabilization resulting from concentration-dependent association or by the interaction of charged residues with the helix dipole. Our results are not predicted by the parameters for alanine and lysine that have been determined by the "host-guest" method: these parameters predict that a 16-residue peptide should not show measurable .alpha.-helix formation. Analysis of the role of the hydrophobic interaction in .alpha.-helix formation [Richards, F. M. and Richmond, T. (1978) in Molecular Interactions and Activity in Proteins, Ciba Foundation Symposium 60, ed. Wolstenholme, G. E. (Excepta Medica Amsterdam), pp. 23-25] does not show an unusually strong hydrophobic interaction in a helical block of alanine residues. The likely explanation for our results is, therefore, that individual alanine residues have a high helical potential. It is not yet known whether any other amino acids show this property, and the origin of this property is also unknown.