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User:Tilman Schirmer/Sandbox 100
From Proteopedia
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A polypeptide chain with a repetition of identical phi-psi torsion angles yields a helical structure. | A polypeptide chain with a repetition of identical phi-psi torsion angles yields a helical structure. | ||
| - | phi-psi = (180<sup>o</sup>, 180<sup>o</sup>) | + | phi-psi = (180<sup>o</sup>, 180<sup>o</sup>), fully extended chain: |
<scene name='User:Tilman_Schirmer/Sandbox_100/Extended/2'>model</scene>, | <scene name='User:Tilman_Schirmer/Sandbox_100/Extended/2'>model</scene>, | ||
<scene name='User:Tilman_Schirmer/Sandbox_100/Extended/3'> Calpha-trace</scene><br> | <scene name='User:Tilman_Schirmer/Sandbox_100/Extended/3'> Calpha-trace</scene><br> | ||
| - | phi-psi = (-140<sup>o</sup>, 130<sup>o</sup>) | + | phi-psi = (-140<sup>o</sup>, 130<sup>o</sup>), extended chain, |
<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 β-strand conformation found in beta-sheets, note the <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>left-twist</scene> for a polypeptide with this conformation <br> | <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/2'>Calpha-trace</scene>; this is the β-strand conformation found in beta-sheets, note the <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>left-twist</scene> for a polypeptide with this conformation <br> | ||
| Line 18: | Line 18: | ||
<scene name='User:Tilman_Schirmer/Sandbox_100/Elongated_helix/2'>Calpha-trace</scene>; note that there are clashes (where?)<br> | <scene name='User:Tilman_Schirmer/Sandbox_100/Elongated_helix/2'>Calpha-trace</scene>; note that there are clashes (where?)<br> | ||
| - | phi-psi = (-60<sup>o</sup>, -40<sup>o</sup>), | + | phi-psi = (-60<sup>o</sup>, -40<sup>o</sup>), α-helix: |
<scene name='User:Tilman_Schirmer/Sandbox_100/Helix/1'>model</scene>, | <scene name='User:Tilman_Schirmer/Sandbox_100/Helix/1'>model</scene>, | ||
| - | <scene name='User:Tilman_Schirmer/Sandbox_100/Helix/2'>Calpha-trace</scene> | + | <scene name='User:Tilman_Schirmer/Sandbox_100/Helix/2'>Calpha-trace</scene><br> |
| - | phi-psi = (-50<sup>o</sup>, -26<sup>o</sup>), | + | phi-psi = (-50<sup>o</sup>, -26<sup>o</sup>),3<sub>10</sub> helix: |
<scene name='User:Tilman_Schirmer/Sandbox_100/310helix/1'>model</scene>, | <scene name='User:Tilman_Schirmer/Sandbox_100/310helix/1'>model</scene>, | ||
| - | <scene name='User:Tilman_Schirmer/Sandbox_100/310helix/2'>Calpha-trace</scene> | + | <scene name='User:Tilman_Schirmer/Sandbox_100/310helix/2'>Calpha-trace</scene> <br> |
Revision as of 19:44, 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.
phi-psi = (180o, 180o), fully extended chain:
,
phi-psi = (-140o, 130o), extended chain,
,
; this is the β-strand conformation found in beta-sheets, note the for a polypeptide with this conformation
phi-psi = (70o, -180o),
,
; note that there are clashes (where?)
phi-psi = (-60o, -40o), α-helix:
,
phi-psi = (-50o, -26o),310 helix:
,
