A helix propensity scale based on experimental studies of peptides and proteins
A helix propensity scale based on experimental studies of peptides and proteins
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DOI：
10.1016/s0006-3495(98)77529-0
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发表时间：
1998-07-01
影响因子：
3.4
通讯作者：
Scholtz, JM
中科院分区：
文献类型：
--
作者：
Pace, CN;Scholtz, JM
球状蛋白平均含有30%的α -螺旋，这是最常见的二级结构。有些氨基酸比其他氨基酸更频繁地出现在α -螺旋中；这种倾向被称为螺旋倾向。在这里，我们推导出了一个螺旋倾向尺度，用于溶剂暴露在或螺旋中间位置的残留物。该量表是基于测量螺旋倾向在11个系统，包括蛋白质和肽。丙氨酸的螺旋倾向最高，除脯氨酸外，甘氨酸的螺旋倾向最低，大约比丙氨酸低1 hcal/mol。根据我们的分析，氨基酸的螺旋倾向如下（kcal/mol）： Ala = 0, Leu = 0.21,Arg = 0.21, Met = 0.24, Lys = 0.26, Gln = 0.39, Glu = 0.40, Ile = 0.41, Trp = 0.49, Ser = 0.50, Tyr = 0.53, Phe = 0.54, Val = 0.61, His = 0.61, Asn = 0.65, Thr = 0.66, Cys = 0.68, Asp = 0.69, Gly = 1。
The average globular protein contains 30% alpha-helix, the most common type of secondary structure. Some amino acids occur more frequently in alpha-helices than others; this tendency is known as helix propensity. Here we derive a helix propensity scale for solvent-exposed residues in the middle positions of or-helices. The scale is based on measurements of helix propensity in 11 systems, including both proteins and peptides. Alanine has the highest helix propensity, and, excluding proline, glycine has the lowest, similar to 1 hcal/mol less favorable than alanine. Based on our analysis, the helix propensities of the amino acids are as follows (kcal/mol): Ala = 0, Leu = 0.21,Arg = 0.21, Met = 0.24, Lys = 0.26, Gln = 0.39, Glu = 0.40, Ile = 0.41, Trp = 0.49, Ser = 0.50, Tyr = 0.53, Phe = 0.54, Val = 0.61, His = 0.61, Asn = 0.65, Thr = 0.66, Cys = 0.68, Asp = 0.69, and Gly = 1.