Alpha helix
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A common motif in the secondary structure of proteins, the alpha helix (α-helix) is a right-handed coiled or spiral conformation, in which every backbone N-H group donates a hydrogen bond to the backbone C=O group of the amino acid four residues earlier (<math>i+4 \rightarrow i</math> hydrogen bonding). This secondary structure is also sometimes called a classic Pauling–Corey–Branson alpha helix (see below). 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.
- See also: Wikipedia
- Related: Folding (chemistry), Beta sheet, Knobs into holes packing, Secondary structure, Tertiary structure, Davydov soliton
| NetSurfP - Secondary Structure and Surface Accessi... NetSurfP - Secondary Structure and Surface Accessibility predictor www.cbs.dtu.dk/services/NetSurfP/ - Web |
| Interactive model of an α-helix Interactive model of an α-helix www2.ufp.pt/~pedros/anim/2frame_helixen.htm - Web |
| Animated details of α-helix Animated details of α-helix www3.interscience.wiley.com:8100/.../8-11.html - Web |
Gallery for «Alpha helix»
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| Artist Julie Newdoll's website Artist Julie Newdoll's website www.brushwithscience.com - Web |
| Artist Julian Voss-Andreae's website Artist Julian Voss-Andreae's website www.JulianVossAndreae.com - Web |
