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Helix
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Helix

A helix (pl: helixes or helices) is a type of smooth space curve, i.e. a curve in three-dimensional space. It has the property that the tangent line at any point makes a constant angle with a fixed line called the axis. Examples of helices are coil springs and the handrails of spiral staircases. A "filled-in" helix – for example, a spiral ramp – is called a helicoid. Helices are important in biology, as the DNA molecule is formed as two intertwined helices, and many proteins have helical substructures, known as alpha helices. The word helix comes from the Greek word ἕλιξ, "twisted, curved".

Types

Helices can be either right-handed or left-handed. With the line of sight along the helix's axis, if a clockwise screwing motion moves the helix away from the observer, then it is called a right-handed helix; if towards the observer, then it is a left-handed helix. Handedness (or chirality) is a property of the helix, not of the perspective: a right-handed helix cannot be turned to look like a left-handed one unless it is viewed in a mirror, and vice versa.

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Alpha helix

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 alpha 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.

Discovery

In the early 1930s, William Astbury showed that there were drastic changes in the X-ray fiber diffraction of moist wool or hair fibers upon significant stretching. The data suggested that the unstretched fibers had a coiled molecular structure with a characteristic repeat of ~5.1 ångströms (0.51 nm).

This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Alpha_helix

Pi helix

A pi helix (or π-helix) is a type of secondary structure found in proteins. Although once thought to be rare, short π-helices are found in 15% of known protein structures and are believed to be an evolutionary adaptation derived by the insertion of a single amino acid into an α-helix. Because such insertions are highly destabilizing, the formation of π-helices would tend to be selected against unless it provided some functional advantage to the protein. π-helices therefore are typically found near functional sites of proteins.

Standard structure

The amino acids in a standard π-helix are arranged in a right-handed helical structure. Each amino acid corresponds to an 87° turn in the helix (i.e., the helix has 4.1 residues per turn), and a translation of 1.15 Å (=0.115 nm) along the helical axis. Most importantly, the N-H group of an amino acid forms a hydrogen bond with the C=O group of the amino acid five residues earlier; this repeated i+5→i hydrogen bonding defines a π-helix. Similar structures include the 3₁₀ helix (i+3→i hydrogen bonding) and the α-helix (i+4→i hydrogen bonding).

This page contains text from Wikipedia, the Free Encyclopedia - https://wn.com/Pi_helix

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Latest News for: Α helices

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Latest News for: Α helices

Astonishing Video Shows 2 Million Kilometer Helical Structure Emerge From The Sun

First helically dichroic hollow-core fiber demonstrated: New waveguide promises optical advances

Observations of a nearby pulsar wind nebula reveal a radio jet feature with a helical ...

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