Richardson J S, Richardson D C
Department of Biochemistry, Duke University, Durham, NC 27710.
Science. 1988 Jun 17;240(4859):1648-52. doi: 10.1126/science.3381086.
A definition based on alpha-carbon positions and a sample of 215 alpha helices from 45 different globular protein structures were used to tabulate amino acid preferences for 16 individual positions relative to the helix ends. The interface residue, which is half in and half out of the helix, is called the N-cap or C-cap, whichever is appropriate. The results confirm earlier observations, such as asymmetrical charge distributions in the first and last helical turn, but several new, sharp preferences are found as well. The most striking of these are a 3.5:1 preference for Asn at the N-cap position, and a preference of 2.6:1 for Pro at N-cap + 1. The C-cap position is overwhelmingly dominated by Gly, which ends 34 percent of the helices. Hydrophobic residues peak at positions N-cap + 4 and C-cap - 4.
基于α-碳位置的定义以及来自45种不同球状蛋白质结构的215个α螺旋样本,用于列出相对于螺旋末端16个单独位置的氨基酸偏好。处于螺旋内外各一半的界面残基,根据情况称为N-帽或C-帽。结果证实了早期的观察结果,例如在第一个和最后一个螺旋圈中的不对称电荷分布,但也发现了一些新的、明显的偏好。其中最显著的是在N-帽位置Asn的偏好为3.5:1,在N-帽 + 1位置Pro的偏好为2.6:1。C-帽位置绝大多数由Gly占据,它终止了34%的螺旋。疏水残基在N-帽 + 4和C-帽 - 4位置达到峰值。