Helices in Proteins

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(add text to page)
(adding synchronization)
Line 52: Line 52:
</table>
</table>
 +
 +
<jmol>
 +
<jmolCheckbox>
 +
<target>all</target>
 +
<scriptWhenChecked>set syncMouse on;set syncScript on;sync * on;</scriptWhenChecked>
 +
<scriptWhenUnchecked>sync * off;</scriptWhenUnchecked>
 +
<text>synchronize the 3 models</text>
 +
</jmolCheckbox>
 +
</jmol>

Revision as of 16:26, 6 November 2010

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
Drag the structure with the mouse to rotate
Drag the structure with the mouse to rotate
Drag the structure with the mouse to rotate

310
3 residues/turn
rise 0.20 nm/residue
helix pitch 0.60 nm
H bonds: Ni+3 → Oi
φ = -49°, ψ = -26°

3.613
3.6 residues/turn
rise 0.15 nm/residue
helix pitch 0.54 nm
H bonds: Ni+4 → Oi
φ = -60°, ψ = -45°

4.416
4.4 residues/turn
rise ~0.115 nm/residue
helix pitch ~0.41 nm
H bonds: Ni+5 → Oi
φ = -55°, ψ = -70° (approx.)

Proteopedia Page Contributors and Editors (what is this?)

Angel Herraez, Eric Martz, Karsten Theis, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/Helices_in_Proteins"
Personal tools