Helices in Proteins: Difference between revisions
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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<ref name=" | 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 name="jourdan">PMID: 12910453</ref><ref name="moradi">PMID: 19923435</ref>. (It is left-handed when formed with D-amino acids<ref name="jourdan" /><ref name="moradi" />.) When viewed from either end, right-handed helices turn clockwise when followed away from you. | ||
==See Also== | ==See Also== | ||
Revision as of 23:35, 11 April 2011
Helical conformations in proteinsHelical 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
|
3.613
|
4.416
|
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][2]. (It is left-handed when formed with D-amino acids[1][2].) When viewed from either end, right-handed helices turn clockwise when followed away from you.
See AlsoSee Also
- Alpha helix at Wikipedia.
ReferencesReferences
- ↑ 1.0 1.1 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
- ↑ 2.0 2.1 Moradi M, Babin V, Roland C, Darden TA, Sagui C. Conformations and free energy landscapes of polyproline peptides. Proc Natl Acad Sci U S A. 2009 Dec 8;106(49):20746-51. Epub 2009 Nov 18. PMID:19923435 doi:10.1073/pnas.0906500106