User:Tilman Schirmer/Sandbox 100

(Difference between revisions)

Revision as of 15:09, 23 March 2009

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 = (-140^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

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: ,

An α-Helix is stabilized by main-chain between O_i and N_i+4. With .

With .

With .

@@ Line 86: / Line 86: @@
 <scene name='User:Tilman_Schirmer/Sandbox_100/Beta_sheets_backbone/2'>Beta strands C-alpha trace</scene>
+<scene name='User:Tilman_Schirmer/Sandbox_100/Beta_sheets_bas/1'>Beta strands ball and stick</scene>
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@@ Line 92: / Line 94: @@
 <scene name='User:Tilman_Schirmer/Sandbox_100/Alpha_helix_backbone/3'>Alpha helix C-alpha trace</scene>
+<scene name='User:Tilman_Schirmer/Sandbox_100/Alpha_helix_bas/1'>Alpha helix ball and stick</scene>
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