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User:Tilman Schirmer/Sandbox 100
From Proteopedia
(→Secondary structure of proteins) |
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[[User:Tilman Schirmer/Sandbox 110|Repetitive torsion angles]] | [[User:Tilman Schirmer/Sandbox 110|Repetitive torsion angles]] | ||
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[[User:Tilman Schirmer/Sandbox 111|α-Helix]] | [[User:Tilman Schirmer/Sandbox 111|α-Helix]] | ||
| + | |||
[[User:Tilman Schirmer/Sandbox 112|parallel β-sheet]] | [[User:Tilman Schirmer/Sandbox 112|parallel β-sheet]] | ||
| - | [[User:Tilman Schirmer/Sandbox 113|antiparallel β-sheet]] | ||
| - | + | [[User:Tilman Schirmer/Sandbox 113|antiparallel β-sheet]] | |
| - | parallel β-sheet | ||
| - | + | ---- | |
| + | ---- | ||
Revision as of 08:17, 10 November 2009
Contents |
Secondary structure of proteins
outline:
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
|
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
