Helices in Proteins
From Proteopedia
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| - | The alpha helix is by far the most common helix. Note that it is a right-handed helix when formed with the common L-amino acids. (It is left-handed when formed with D-amino acids.) When viewed from either end, right-handed helices turn clockwise when followed away from you. | + | The alpha helix is by far the most common helix. Note that it is a right-handed helix when formed with the common L-amino acids<ref>PMID: 12910453</ref>. (It is left-handed when formed with D-amino acids.) When viewed from either end, right-handed helices turn clockwise when followed away from you. |
==See Also== | ==See Also== | ||
Revision as of 20:30, 11 April 2011
Helical conformations in proteins
This page illustrates the 3 most common helical conformations (secondary structures) found in proteins.
All are decapeptide segments extracted from actual protein structures in the PDB. They are shown using the same scale, for a better comparison (as a consequence, zoom in the Jmol applets is disabled).
| 310 helix | alpha helix | pi helix | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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310
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3.613
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4.416
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The alpha helix is by far the most common helix. Note that it is a right-handed helix when formed with the common L-amino acids[1]. (It is left-handed when formed with D-amino acids.) When viewed from either end, right-handed helices turn clockwise when followed away from you.
See Also
- Alpha helix at Wikipedia.
References
- ↑ Jourdan F, Lazzaroni S, Mendez BL, Lo Cantore P, de Julio M, Amodeo P, Iacobellis NS, Evidente A, Motta A. A left-handed alpha-helix containing both L- and D-amino acids: the solution structure of the antimicrobial lipodepsipeptide tolaasin. Proteins. 2003 Sep 1;52(4):534-43. PMID:12910453 doi:http://dx.doi.org/10.1002/prot.10418
