This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
User:Tilman Schirmer/Sandbox 100
From Proteopedia
| Line 24: | Line 24: | ||
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/ | + | <scene name='User:Tilman_Schirmer/Sandbox_100/310helix/2'>Calpha-trace</scene>; this is the conformation of a 3<sub>10</sub> helix<br> |
Revision as of 18:10, 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
