helix

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Related to a-helix: alpha helix

helix

1. a curve that lies on a cylinder or cone, at a constant angle to the line segments making up the surface; spiral
2. the incurving fold that forms the margin of the external ear
3. another name for volute
4. any terrestrial gastropod mollusc of the genus Helix, which includes the garden snail (H. aspersa)

Helix

Any spiral form, particularly a small volute or twist under the abacus of the Corinthian capital.

helix

[′hē‚liks]
(electricity)
A spread-out, single-layer coil of wire, either wound around a supporting cylinder or made of stiff enough wire to be self-supporting.
(mathematics)
A curve traced on a cylindrical or conical surface where all points of the surface are cut at the same angle.
(cell and molecular biology)
A spiral structure with a repeating pattern that characterizes many biological polymers, for example, double-stranded nucleic acids and proteins.

Helix

[′hē‚liks]
(invertebrate zoology)
A genus of pulmonate land mollusks including many of the edible snails; individuals have a coiled shell with a low conical spire.

helix

helix, 1: H
1. Any spiral, particularly a small volute or twist under the abacus of the Corinthian capital.
2. The volute of an Ionic capital.

Helix

A hardware description language from Silvar-Lisco.
References in periodicals archive ?
Although no significant correlation was found in a 5% protein concentration, a transformation from [beta]-sheet to both a-helix and [beta]-turn occurred in SPI heat treated for 30 min and 60 min, leading to an increased surface hydrophobicity, suggesting that the transformation to ordered structure elements (such as [alpha]-helix and [beta]-sheet structures) may be an important factor influencing the surface hydrophobicity.
Lee, "Changes in the amide I FT-IR bands of poly-L-lysine on spray-drying from a-helix, [beta]-sheet or random coil conformations," European Journal of Pharmaceutics and Biopharmaceutics, vol.
A single residue in its natural state cannot be alone folded into a-helix or [beta]-sheet.
These structural changes were expected from the structural differences between residues R and Q compared to H, and also because the residue 168 is almost totally buried in the hydrophobic core of the a-helix 5, with only its tip exposed to the solvent.
In agreement with a report showing that a-helix 1 is cleaved off during the insertion process (Aronson et al., 1999).