Brazhnikov E V, Efimov A V
Mol Biol (Mosk). 2007 May-Jun;41(3):544-55.
The study shows that in coiled-coil proteins the distribution of hydrophobic side-chain rotamers in a- and d-positions of alpha-helices is strongly dependent on the mutual arrangement of the a-helices. In coiled-coil dimers, where a-helices are packed "face-to-face", most side chains occupying a-positions adopt t-rotamers, and those in d-positions adopt g- -rotamers. In tetramers, where alpha-helices are packed "side-by-side", most side chains in a-positions adopt g- -rotamers and those in d-positions adopt t-rotamers. These features can be used for prediction of side-chain rotamers in protein modeling and design.
该研究表明，在卷曲螺旋蛋白中，α螺旋a位和d位的疏水侧链旋转异构体的分布强烈依赖于α螺旋的相互排列。在卷曲螺旋二聚体中，α螺旋“面对面”堆积，占据a位的大多数侧链采用t旋转异构体，而占据d位的侧链采用g-旋转异构体。在四聚体中，α螺旋“并排”堆积，a位的大多数侧链采用g-旋转异构体，d位的侧链采用t旋转异构体。这些特征可用于蛋白质建模和设计中侧链旋转异构体的预测。
