Holak T A, Prestegard J H
Biochemistry. 1986 Sep 23;25(19):5766-74. doi: 10.1021/bi00367a063.
Sequence-specific assignments of 1H NMR resonances were obtained for the backbone protons in acyl carrier protein (ACP) from Escherichia coli, a protein of 77 residues. The observations, in the NOESY spectra, of 1H-1H sequential and medium-range connectivities indicate the presence of three or four alpha-helical segments joined by short sequences of mixed conformations. The observations are used to refine a secondary structure model previously proposed on the basis of a Chou-Fasman algorithm [Rock, C. O., & Cronan, J. E., Jr. (1979) J. Biol. Chem. 254, 9778-9785].
已获得来自大肠杆菌的酰基载体蛋白（ACP，一种由77个残基组成的蛋白质）主链质子的1H NMR共振的序列特异性归属。在NOESY谱中观察到的1H-1H序列和中等距离连接性表明存在由混合构象的短序列连接的三个或四个α-螺旋片段。这些观察结果用于完善先前基于Chou-Fasman算法提出的二级结构模型[Rock, C. O., & Cronan, J. E., Jr. (1979) J. Biol. Chem. 254, 9778-9785]。
