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单词 Helix structure
释义

Helix structure

原声例句
日常生活医学科普

Due to the bond angle of the sugar-phosphate molecules, the linkages will eventually form a double helix structure.

由于糖-磷酸分子的键角,最终形成双螺旋结构。

BBC随身英语(官网版)

Well, just a little thing called the double helix structure of DNA.

好吧, 只是一个叫做 DNA 双螺旋结构的小​​东西。

2023-40

This double helix structure carries the instructions for making all the proteins a cell will ever need.

这种双螺旋结构携带着制造细胞所需的所有蛋白质的指令。

SciSHow 快问快答小科普

To make that iconic double helix structure, the bases of one strand pair up with the bases of another strand.

为了形成标志性的双螺旋结构, 一条链的碱基与另一条链的碱基配对。

科普小杂文

Your DNA is made up of two strains that wrap around each other in the famous double helix structure, to get even more compact and tiny, that DNA is wrapped around little proteins called histones.

你的DNA是由两个菌株组成的,它们以著名的双螺旋结构相互缠绕,变得更加紧密和微小,DNA被包裹在称为组蛋白的小蛋白质上。

202329

Decoding the Blueprint The beauty of DNA lies in its double helix structure, discovered by James Watson and Francis Crick in 1953. Imagine a twisted ladder, where each rung is made of a pair of nitrogen bases.

解码蓝图 DNA 的美妙之处在于它的双螺旋结构,由 James Watson 和 Francis Crick 于 1953 年发现。想象一下一个扭曲的梯子,其中每个梯级都由一对氮碱基组成。

中文百科

Α螺旋 Alpha helix

(重定向自Helix structure)
聚丙氨酸形成的α螺旋结构,侧面观
La liaison hydrogène se fait entre les acides aminés n et n+4
Comparaison vue de dessus d'une hélice α (forme carrée) et d'une hélice 310 (forme triangulaire)

α螺旋是蛋白质的二级结构。它和β折叠一起被称为「规则二级结构」,因为他们都具有重复的Φ和Ψ值(Cα-N夹角和Cα-C夹角)。

α螺旋一般是右手螺旋。在α螺旋中,平均每个螺旋周期包含3.6个氨基酸残基,残基侧链伸向外侧,同一肽链上的每个残基的酰胺氢原子和位于它后面的第4个残基上的羰基氧原子之间形成氢键,N-O距离是2.8Å。这种氢键大致与螺旋轴平行。一条多肽链呈α螺旋构象的推动力就是所有肽键上的酰胺氢和羰基氧之间形成的链内氢键。在水环境中,肽键上的酰胺氢和羰基氧既能形成内部(α螺旋内)的氢键,也能与水分子形成氢键。如果后者发生,多肽链呈现类似变性蛋白质那样的伸展构象。疏水环境对于氢键的形成没有影响,因此,更可能促进α螺旋结构的形成。

英语百科

Alpha helix Α螺旋

(重定向自Helix structure)
Side view of an α-helix of alanine residues in atomic detail. Two hydrogen bonds for the same peptide group are highlighted in magenta; the H to O distance is about 2 Å (0.20 nm). The protein chain runs upward here; that is, its N-terminus is at the bottom and its C-terminus at the top. Note that the sidechains (black stubs) angle slightly downward, toward the N-terminus, while the peptide oxygens (red) point up and the peptide NHs (blue with grey stubs) point down.
Top view of the same helix shown above. Four carbonyl groups are pointing upwards toward the viewer, spaced roughly 100° apart on the circle, corresponding to 3.6 amino-acid residues per turn of the helix.
Contrast of helix end views between α (offset squarish) vs 310 (triangular)
Ramachandran plot (φ,ψ plot), with data points for α-helical residues forming a dense diagonal cluster below and left of center, around the global energy minimum for backbone conformation.[11]

The alpha helix (α-helix) is a common secondary structure of proteins and is a righthand-coiled or spiral conformation (helix) in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier (i+4 \rightarrow i hydrogen bonding). This secondary structure is also sometimes called a classic Pauling–Corey–Branson α-helix (see below). The name 3.613-helix is also used for this type of helix, denoting the number of residues per helical turn, and 13 atoms being involved in the ring formed by the hydrogen bond. Among types of local structure in proteins, the α-helix is the most regular and the most predictable from sequence, as well as the most prevalent.

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