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User:Tilman Schirmer/Sandbox 100
From Proteopedia
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extended chain: phi-psi = (-140<sup>o</sup>, 130<sup>o</sup>), | extended chain: phi-psi = (-140<sup>o</sup>, 130<sup>o</sup>), | ||
<scene name='User:Tilman_Schirmer/Sandbox_100/Beta/1'>model</scene>, | <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/1'>model</scene>, | ||
| - | <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/2'>Calpha-trace</scene>; this is the beta-strand conformation found in beta-sheets | + | <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/2'>Calpha-trace</scene>; this is the beta-strand conformation found in beta-sheets, note the <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>left-twist</scene> of the polypeptide <br> |
Revision as of 13:09, 15 March 2009
Contents |
Secondary structure of proteins
Repetitive torsion angles
A polypeptide chain with a repetition of identical phi-psi torsion angles yields a helical structure.
Examples:
...
Drag the structure with the mouse to rotate fully extended chain: phi-psi = (180o, 180o), ,
extended chain: phi-psi = (-140o, 130o), , ; this is the beta-strand conformation found in beta-sheets, note the of the polypeptide
phi-psi = (70o, -180o), model, Cα-trace; note that there are clashes (where?)
phi-psi = (-60o, -40o), model, Cα-trace; this is the alpha-helical conformation
phi-psi = (-50o, -26o), model, Cα-trace; this is the conformation of a 310 helix
