User:Tilman Schirmer/Sandbox 110

(Difference between revisions)

Revision as of 13:21, 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

phi-psi = (-140^o, 130^o), extended chain: , ; t..

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 = (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: ,

@@ Line 22: / Line 22: @@
 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/2'>Calpha-trace</scene>; this is the '''β-strand''' conformation found in beta-sheets <br>
+<scene name='User:Tilman_Schirmer/Sandbox_100/Beta/2'>Calpha-trace</scene>; t.. <br>
 Note: <br>