Definition, Betydelse & Anagram | Engelska ordet HELICES

Definition av HELICES

1. böjningsform av helix

Exempel på hur man kan använda HELICES i en mening

• The two most common secondary structural elements are alpha helices and beta sheets, though beta turns and omega loops occur as well.
• A Corinthian capital may be seen as an enriched development of the Ionic capital, though one may have to look closely at a Corinthian capital to see the Ionic volutes ("helices"), at the corners, perhaps reduced in size and importance, scrolling out above the two ranks of stylized acanthus leaves and stalks ("cauliculi" or caulicoles), eight in all, and to notice that smaller volutes scroll inwards to meet each other on each side.
• In proteins aspartate sidechains are often hydrogen bonded to form asx turns or asx motifs, which frequently occur at the N-termini of alpha helices.
• Threonine sidechains are often hydrogen bonded; the most common small motifs formed are based on interactions with serine: ST turns, ST motifs (often at the beginning of alpha helices) and ST staples (usually at the middle of alpha helices).
• While long, thin strips may be the most common, many varieties of noodles are cut into waves, helices, tubes, strings, or shells, or folded over, or cut into other shapes.
• This 'globin fold' typically consists of eight alpha helices, although some proteins have additional helix extensions at their termini.
• Most suitably equipped metalworking lathes can also be used to produce most solids of revolution, plane surfaces and screw threads or helices.
• 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.
• In semiconservative replication, when the double-stranded DNA helix is replicated, each of the two new double-stranded DNA helices consisted of one strand from the original helix and one newly synthesized.
• In the leucine zipper motif, a repeating pattern of leucines on the facing sides of two adjacent helices is highly predictive of the motif.
• Each monomer has seven transmembrane alpha helices and an extracellular-facing, two-stranded beta sheet.
• The histone fold is a structural motif located near the C-terminus of histone proteins, characterized by three alpha helices separated by two loops.
• For example, the "All-α proteins" class contains >280 distinct folds, including: Globin-like (core: 6 helices; folded leaf, partly opened), long alpha-hairpin (2 helices; antiparallel hairpin, left-handed twist) and Type I dockerin domains (tandem repeat of two calcium-binding loop-helix motifs, distinct from the EF-hand).
• The recognition and binding to DNA by helix-turn-helix proteins is done by the two α helices, one occupying the N-terminal end of the motif, the other at the C-terminus.
• In addition to the eight central β-barrels and eight peripheral α-helices, ADA also contains five additional helices: residues 19-76 fold into three helices, located between β1 and α1 folds; and two antiparallel carboxy-terminal helices are located across the amino-terminal of the β-barrel.
• 14-3-3 proteins are structurally similar to the Tetratrico Peptide Repeat (TPR) superfamily, which generally have 9 or 10 alpha helices, and usually form homo- and/or hetero-dimer interactions along their amino-termini helices.
• The transmembrane helices from the 4 domains line up to form the channel proper; S5 and S6 helices are thought to line the inner pore surface, while S1–4 helices have roles in gating and voltage sensing (S4 in particular).
• Protein structures are usually determined from either 2-dimensional crystals (sheets or helices), polyhedrons such as viral capsids, or dispersed individual proteins.
• Each hERG subunit consists of 6 transmembrane alpha helices, numbered S1-S6, a pore helix situated between S5 and S6, and cytoplasmically located N- and C-termini.
• Mindbender was a pseudo mirror-image of Dreier Looping, and was slightly taller, with additional helices at the end of the ride.

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