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User:Tilman Schirmer/Sandbox 100

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(Repetitive torsion angles)
(Repetitive torsion angles)
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phi-psi = (-50<sup>o</sup>, -26<sup>o</sup>), '''3<sub>10</sub> helix''':
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> <br>
+
<scene name='User:Tilman_Schirmer/Sandbox_100/310helix/2'>Calpha-trace</scene> <br><br><br><br><br><br>
==== α-Helix ====
==== α-Helix ====

Revision as of 23:35, 19 March 2009

Contents

Secondary structure of proteins

Repetitive torsion angles

Drag the structure with the mouse to rotate

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:

polypeptide forms a with side-chains protruding towards alternating (up, down) directions

the polypeptide main-chain is as can been seen when looking along the chain


phi-psi = (70o, 180o): , ; note that there are clashes (where?)


phi-psi = (-60o, -40o), α-helix: ,


phi-psi = (-50o, -26o), 310 helix: ,





α-Helix

β-sheet

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Tilman Schirmer

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