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User:Tilman Schirmer/Sandbox 100
From Proteopedia
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phi-psi = (-50<sup>o</sup>, -26<sup>o</sup>), | phi-psi = (-50<sup>o</sup>, -26<sup>o</sup>), | ||
<scene name='User:Tilman_Schirmer/Sandbox_100/310helix/1'>model</scene>, | <scene name='User:Tilman_Schirmer/Sandbox_100/310helix/1'>model</scene>, | ||
| - | <scene name='User:Tilman_Schirmer/Sandbox_100/310helix/1'> | + | <scene name='User:Tilman_Schirmer/Sandbox_100/310helix/1'>Calpha-trace</scene>; this is the conformation of a 3<sub>10</sub> helix<br> |
Revision as of 17:40, 15 March 2009
Contents |
Secondary structure of proteins
Repetitive torsion angles
|
A polypeptide chain with a repetition of identical phi-psi torsion angles yields a helical structure.
fully extended chain: phi-psi = (180o, 180o),
,
extended chain: phi-psi = (-140o, 130o),
,
; this is the beta-strand conformation found in beta-sheets, note the for a polypeptide with this conformation
phi-psi = (70o, -180o),
,
; note that there are clashes (where?)
phi-psi = (-60o, -40o),
,
; this is the alpha-helical conformation
phi-psi = (-50o, -26o),
,
; this is the conformation of a 310 helix
