A MODEL PEPTIDE WITH ENHANCED HELICITY
A MODEL PEPTIDE WITH ENHANCED HELICITY
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DOI：
10.1021/bi00231a020
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发表时间：
1991-04-30
期刊：
影响因子：
2.9
通讯作者：
STELLWAGEN, E
中科院分区：
文献类型：
--
作者：
MERUTKA, G;SHALONGO, W;STELLWAGEN, E
改变了模型单体肽乙酰A（EAAAK）3Aamide的序列，以加快肽浓度的测量并提高其螺旋含量。 用色氨酸残基取代N-末端丙氨酸残基提供了用于测量肽浓度的方便发色团，而不减少螺旋含量。 用精氨酸残基取代三个赖氨酸残基增强了螺旋含量，而不损失它们的静电贡献。 将肽乙酰基W（EAAAR）（n）Aamide中的EAAAR序列单元的数目从3个增加到5个，表明完全螺旋肽的预期光谱特征非常接近。
The sequence of a model monomeric peptide, acetylA(EAAAK)3Aamide was altered to expedite measurement of peptide concentration and to enhance its fractional helical content. Replacement of the N-terminal alanine residue with a tryptophan residue provides a convenient chromophore for measurement of peptide concentration without diminishing the helical content. Replacement of the three lysine residues with arginine residues enhances the helical content without loss of their electrostatic contributions. Increasing the number of EAAAR sequence units in the peptide acetylW(EAAAR)(n)Aamide from three to five indicates that the spectral features anticipated for a completely helical peptide are closely approached.