User:Tilman Schirmer/Sandbox 110

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polypeptide forms a <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/4'>zig-zag</scene> 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> with side-chains protruding towards alternating (up, down) directions<br>
-
the polypeptide main-chain is <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>right-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>
the <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/5'>side-chains</scene> point towards alternate directions<br>
the <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/5'>side-chains</scene> point towards alternate directions<br>

Revision as of 08:31, 24 February 2010

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Repetitive torsion angles

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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

the point towards alternate directions


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


phi-psi = (-60o, -40o), α-helix: ,


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


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Tilman Schirmer

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