Dihedral/Dihedral angles in proteins

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(fix the script running (path was wrong))
Line 10: Line 10:
Bright magenta cylinders are displayed where neighbour atoms collide (hence there is an unfavourable conformation for those ϕ, ψ values).
Bright magenta cylinders are displayed where neighbour atoms collide (hence there is an unfavourable conformation for those ϕ, ψ values).
-
Animation of rotation:
+
Animation of rotation for ϕ:
<jmol>
<jmol>
<jmolButton>
<jmolButton>
Line 31: Line 31:
<jmol>
<jmol>
<jmolApplet>
<jmolApplet>
-
<size>400</size>
+
<size>500</size>
<color>white</color>
<color>white</color>
<uploadedFileContents>1iy4_34-36.pdb</uploadedFileContents>
<uploadedFileContents>1iy4_34-36.pdb</uploadedFileContents>

Revision as of 16:46, 14 July 2016

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

Dihedral angles in proteins: Phi and Psi

The model displayed on the right is a tripeptide (Trp34–Glu35–Ser36 within the protein lysozyme). This page illustrates the meaning of phi (ϕ) and psi (ψ) angles, both around the alpha carbon of the central residue (Glu35).

You can run animations that continuously rotate the model changing one of the angles, or use the slider or controls to manually progress through different values of the angles. Bright magenta cylinders are displayed where neighbour atoms collide (hence there is an unfavourable conformation for those ϕ, ψ values).

Animation of rotation for ϕ:

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Angel Herraez

Personal tools