Helices in Proteins
From Proteopedia
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<br />H bonds: N<sub>i+3</sub> → O<sub>i</sub> | <br />H bonds: N<sub>i+3</sub> → O<sub>i</sub> | ||
<br />φ = -49°, ψ = -26° | <br />φ = -49°, ψ = -26° | ||
| - | <br />[[3l79]]: 514-525 | + | <br />from [[3l79]]: 514-525 |
</td> | </td> | ||
<td style="vertical-align:top;text-align:center;"> | <td style="vertical-align:top;text-align:center;"> | ||
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<br />H bonds: N<sub>i+4</sub> → O<sub>i</sub> | <br />H bonds: N<sub>i+4</sub> → O<sub>i</sub> | ||
<br />φ = -60°, ψ = -45° | <br />φ = -60°, ψ = -45° | ||
| - | <br />1hho chain B: 5-16 | + | <br />from [[1hho]] chain B: 5-16 |
</td> | </td> | ||
<td style="vertical-align:top;text-align:center;"> | <td style="vertical-align:top;text-align:center;"> | ||
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<br />H bonds: N<sub>i+5</sub> → O<sub>i</sub> | <br />H bonds: N<sub>i+5</sub> → O<sub>i</sub> | ||
<br />φ = -55°, ψ = -70° (approx.) | <br />φ = -55°, ψ = -70° (approx.) | ||
| - | <br />[[2qd3]] chain A: 346-357 | + | <br />from [[2qd3]] chain A: 346-357 |
</td> | </td> | ||
</tr> | </tr> | ||
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| - | The alpha helix | + | 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="novotny">PMID: 15740737</ref><ref name="jourdan">PMID: 12910453</ref><ref name="moradi">PMID: 19923435</ref>. (It is left-handed when formed with D-amino acids<ref name="novotny" /><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== | ||
| - | *[[Alpha helix]] | + | *[[Alpha helix|Alpha helix (1)]] and also [[User:Karsten Theis/alpha helix|Alpha helix (2)]] |
| - | *[https://chemapps.stolaf.edu/jmol/jsmol/helix.htm | + | *[https://chemapps.stolaf.edu/jmol/jsmol/helix.htm JSmol helix builder] |
| + | *[http://wiki.jmol.org/index.php/Recycling_Corner/Alpha_Helix_Generator RIBOZOME - an Alpha Helix Generator] | ||
*[http://en.wikipedia.org/wiki/Alpha_helix Alpha helix] at Wikipedia. | *[http://en.wikipedia.org/wiki/Alpha_helix Alpha helix] at Wikipedia. | ||
*[https://en.wikipedia.org/wiki/310_helix 3-10 helix] at Wikipedia. | *[https://en.wikipedia.org/wiki/310_helix 3-10 helix] at Wikipedia. | ||
Revision as of 19:18, 2 February 2018
Helical conformations in proteins
This page illustrates the 3 most common helical conformations (among secondary structures) found in proteins.
Each of the three examples below is a decapeptide fragment extracted from an actual protein structure in the PDB. They are shown using the same scale, for a better comparison (as a consequence, zoom in the Jmol applets is disabled).
To re-align the 3 models, either reload this page or click on each of the 3 green 'Reset' links.
| 310 helix | alpha helix | pi helix | ||||||||||||||||||
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Change rendering:
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][3]. (It is left-handed when formed with D-amino acids[1][2][3].) When viewed from either end, right-handed helices turn clockwise when followed away from you.
See Also
- Alpha helix (1) and also Alpha helix (2)
- JSmol helix builder
- RIBOZOME - an Alpha Helix Generator
- Alpha helix at Wikipedia.
- 3-10 helix at Wikipedia.
- Pi helix at Wikipedia.
- Secondary structure
- Protein primary, secondary, tertiary and quaternary structure (slides for teaching)
- Estructuras primaria, secundaria, terciaria y cuaternaria de las proteínas (en formato de presentación)
References
- ↑ 1.0 1.1 Novotny M, Kleywegt GJ. A survey of left-handed helices in protein structures. J Mol Biol. 2005 Mar 25;347(2):231-41. PMID:15740737 doi:10.1016/j.jmb.2005.01.037
- ↑ 2.0 2.1 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
- ↑ 3.0 3.1 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
