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User:Tilman Schirmer/Sandbox 100

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(Repetitive torsion angles)
(Repetitive torsion angles)
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Note: <br>
Note: <br>
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polypeptide forms a scene name=<scene name='User:Tilman_Schirmer/Sandbox_100/Beta/4'>zig-zag</scene>zig-zag with side-chains protruding towards alternating (up, down) directions<br>
+
 
 +
polypeptide forms a <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/4'>zig-zag</scene>zig-zag with side-chains protruding towards alternating (up, down) directions<br>
 +
 
the polypeptide main-chain is <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>left-twisted</scene> as can been seen when looking along the chain <br>
the polypeptide main-chain is <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>left-twisted</scene> as can been seen when looking along the chain <br>

Revision as of 13:57, 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 zig-zag 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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