User:Tilman Schirmer/Sandbox 110

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Revision as of 13:37, 15 March 2010

A polypeptide chain with a repetition of identical phi-psi torsion angles yields a helical structure.

phi-psi = (180^o, 180^o), fully extended chain: ,

phi-psi = (-110^o, 130^o), 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

Also strands with a are allowed, but they occur less frequent. This strand has phi-psi values of (-140^o, 130^o). See also Ramachandran Plots, http://en.wikipedia.org/wiki/Ramachandran_plot.

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

phi-psi = (-60^o, -40^o), α-helix: ,

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

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-	Also strands with a <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>left-twist</scene> are allowed, but they occur less frequent. This strand has phi-psi values of (-140<sup>o</sup>, 130<sup>o</sup>). See also [[Ramachandran ~~plots~~]], http://en.wikipedia.org/wiki/Ramachandran_plot.	+	Also strands with a <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>left-twist</scene> are allowed, but they occur less frequent. This strand has phi-psi values of (-140<sup>o</sup>, 130<sup>o</sup>). See also [[Ramachandran Plots]], http://en.wikipedia.org/wiki/Ramachandran_plot.

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