Hadley Erik B, Gellman Samuel H
Department of Chemistry, University of Wisconsin, Madison, WI 53706, USA.
J Am Chem Soc. 2006 Dec 27;128(51):16444-5. doi: 10.1021/ja067178r.
Both parallel and antiparallel alpha-helical coiled-coil dimers are common among proteins; however, biophysical scrutiny has focused almost entirely on parallel dimers. We describe the development of a model system that enables efficient and systematic analysis of hydrophobic packing between antiparallel alpha-helices. Our findings reveal significant differences in packing preferences between parallel and antiparallel coiled-coils.
平行和反平行的α-螺旋卷曲螺旋二聚体在蛋白质中都很常见;然而,生物物理研究几乎完全集中在平行二聚体上。我们描述了一个模型系统的开发,该系统能够对反平行α-螺旋之间的疏水堆积进行高效且系统的分析。我们的研究结果揭示了平行和反平行卷曲螺旋在堆积偏好上的显著差异。