Institute of Protein Research, Russian Academy of Sciences, Moscow, Russia.
Methods Mol Biol. 2025;2870:21-40. doi: 10.1007/978-1-0716-4213-9_2.
The packing of α-helices in proteins is determined by both the principle of close packing and the chemical nature of side chains. As shown, amphipathic α-helices having continuous hydrophobic stripes on their surfaces can be packed against each other in two main ways referred to here as face-to-face and side-by-side manners. Three types of the minimal hydrophobic stripes produced by the heptad (7-residue), undecatad (11-residue), and 4-residue repeats in the sequence have been analyzed and their role in packing of α-helices has been considered. A variety of complementary packings of helices having minimal hydrophobic stripes have been modeled and described. This chapter presents a survey of these models as well as many examples of complementary packing of α-helices from known proteins.
蛋白质中 α-螺旋的包装既由紧密堆积的原则决定，也由侧链的化学性质决定。如所示，具有连续疏水面条的两亲性 α-螺旋可以以两种主要方式彼此堆积，这里称为面对面和并排方式。已经分析了七肽（7 个残基）、十一肽（11 个残基）和序列中 4 个残基重复产生的最小疏水面条的三种类型，并考虑了它们在 α-螺旋包装中的作用。已经对具有最小疏水面条的螺旋的各种互补包装进行了建模和描述。本章介绍了这些模型的概述，以及来自已知蛋白质的 α-螺旋互补包装的许多例子。
