An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins .

2023年6月4日 · 在Rosetta中，可以使用 make_helix 命令生成α-螺旋。 该命令需要指定螺旋的起始和结束残基，以及其他相关参数，如螺旋的旋转角度和螺旋的长度。 通过调整这些参数，可以生成不同长度和形状的α-螺旋。 在PyMOL中，可以使用内置的命令或Python脚本生成α-螺旋。 通过选择适当的氨基酸序列和使用合适的命令或脚本，可以在PyMOL中绘制出α-螺旋。 这些方法仅是生成α-螺旋的示例，实际上还有其他方法和工具可用于生成蛋白质的α-螺旋结构。 具体方法的 …

α-螺旋（Alpha-helix）是蛋白质中最重要的一种局部规则结构形式，其特点是在多肽链中， 每个氨基酸残基的羰基（C=O）和氨基（N-H）基团参与形成氢键。

α螺旋（alpha helix (α-helix)；Pauling–Corey–Branson α-helix；3.613-helix）是蛋白质中最常见最典型和含量最丰富的二级结构。 它和 β折叠 因肽段每个二面角Φ和Ψ值都处于同一或几乎同一数值而被称为规正二级结构（C α -N夹角和C α -C夹角）。

2023年9月21日 · The two common secondary structures encountered in proteins are (\(\alpha\)-helix and \(\beta\)-pleated sheet. The other portions of the polymer backbone that are regular but not repetitive are called random coils. Triple-helix is another common secondary structure found in collagen proteins in connective tissues.

An alpha helix is an element of secondary structure in which the amino acid chain is arranged in a spiral. The kinemage linked above shows an individual alpha helix, viewed from the N-terminal end to resemble the "helical wheel" (see figure below). The O and N atoms of the helix main chain are shown as red and blue balls, respectively.

Describe the idealized geometries of different helical types—alpha (α), 3₁₀, and pi (π) helices—including parameters such as residues per turn (n), pitch, and the characteristic phi/psi angles. Compare and contrast the alpha helix with the 3₁₀ and pi helices in terms of stability, dimensions, and side chain orientation.

2016年12月5日 · We present an alternative coordinate system that describes helical conformations in terms of residues per turn (ρ) and angle (ϑ) between backbone carbonyls relative to the helix direction ...

Representative sequences have magenta names and they are colored according to predicted secondary structures (red: alpha-helix, blue: beta-strand). If the sequences are in aligned order, the sequences with black names directly under a representative sequence are in the same pre-aligned group and are aligned in a fast way.

the α−helix is basically that of circular staircase with the polypeptide backbone winding in a right-handed, stair-step fashion from one amino acid AA residue to the next along its corresponding AA sequence, i.e., the primary structure. The symmetrical stair-step motif of the α−helix classifies it as a secondary structure, i.e., a