User:Tilman Schirmer/Sandbox 100
From Proteopedia
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polypeptide forms a <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/4'>zig-zag</scene> with side-chains protruding towards alternating (up, down) directions<br> | polypeptide forms a <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/4'>zig-zag</scene> with side-chains protruding towards alternating (up, down) directions<br> | ||
| - | the polypeptide main-chain is <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'> | + | the polypeptide main-chain is <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/3'>right-twisted</scene> as can been seen when looking along the chain <br> |
the <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/5'>side-chains</scene> point towards alternate directions<br> | the <scene name='User:Tilman_Schirmer/Sandbox_100/Beta/5'>side-chains</scene> point towards alternate directions<br> | ||
Revision as of 21:24, 23 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.
phi-psi = (180o, 180o), fully extended chain:
,
phi-psi = (-140o, 130o), 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 = (70o, 180o):
,
; note that there are clashes (where?)
phi-psi = (-60o, -40o), α-helix:
,
phi-psi = (-50o, -26o), 310 helix: ,
α-Helix
|
An α-Helix is stabilized by main-chain between Oi and Ni+4. With .
parallel β-sheet
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With .
antiparallel β-sheet
|
With .
Anatomy of a protein
|
Response regulator receiver (Rec) domain. See also 1tmy.
The rest are the irregular .
Notes
see also http://proteopedia.org/wiki/index.php/User:James_D_Watson/Structural_Templates
