一种基于肽和蛋白质实验研究的螺旋倾向量表。
A helix propensity scale based on experimental studies of peptides and proteins.
作者信息
Pace C N, Scholtz J M
机构信息
Department of Medical Biochemistry and Genetics, Texas A&M University, College Station, Texas 77843-1114, USA.
出版信息
Biophys J. 1998 Jul;75(1):422-7. doi: 10.1016/s0006-3495(98)77529-0.
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 alpha-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, approximately 1 kcal/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.
普通的球状蛋白质含有30%的α-螺旋，这是最常见的二级结构类型。一些氨基酸在α-螺旋中出现的频率比其他氨基酸更高；这种趋势被称为螺旋倾向。在此，我们推导了α-螺旋中间位置溶剂暴露残基的螺旋倾向量表。该量表基于对11个系统（包括蛋白质和肽）中螺旋倾向的测量。丙氨酸具有最高的螺旋倾向，除脯氨酸外，甘氨酸的螺旋倾向最低，比丙氨酸约低1千卡/摩尔。基于我们的分析，氨基酸的螺旋倾向如下（千卡/摩尔）：丙氨酸 = 0，亮氨酸 = 0.21，精氨酸 = 0.21，甲硫氨酸 = 0.24，赖氨酸 = 0.26，谷氨酰胺 = 0.39，谷氨酸 = 0.40，异亮氨酸 = 0.41，色氨酸 = 0.49，丝氨酸 = 0.50，酪氨酸 = 0.53，苯丙氨酸 = 0.54，缬氨酸 = 0.61，组氨酸 = 0.61，天冬酰胺 = 0.65，苏氨酸 = 0.66，半胱氨酸 = 0.68，天冬氨酸 = 0.69，甘氨酸 = 1。
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