Protein Structural Motifs: The Beta Turn
The
-turn
(1__ - 2 PRO -3 GLY - __ )
a simple protein structural motif
generally found on protein surfaces
turns the backbone around by 180 degrees to fold back on itself
links two anti-parallel two beta strands
that are adjacent in primary structure,
that are adjacent in secondary structure
is a short loop of two to five amino acids
frequently contains glycine at position 3, (small H side chain allows
extreme phi-psi).
frequently contains proline at position 2, (P forces the backbone into the
appropriate conformation)
F
i
g
u
r
e
6
-
1
4
Make a table of delta phi/delta psi, to compare type I and type II
In the realm of protein structure, the beta turn plays a crucial role in folding patterns. This simple motif involves a 180-degree turn in the backbone, linking adjacent beta strands. Typically consisting of 2 to 5 amino acids, with glycine often at position 3 and proline at position 2, the beta turn influences the overall conformation and stability of proteins. By comparing the delta phi and delta psi values between Type I and Type II beta turns, we gain insights into their structural differences and functional implications.
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Presentation Transcript
The -turn (1__ - 2 PRO -3 GLY - __ ) a simple protein structural motif generally found on protein surfaces turns the backbone around by 180 degrees to fold back on itself links two anti-parallel two beta strands that are adjacent in primary structure, that are adjacent in secondary structure is a short loop of two to five amino acids frequently contains glycine at position 3, (small H side chain allows extreme phi-psi). frequently contains proline at position 2, (P forces the backbone into the appropriate conformation)
Make a table of delta phi/delta psi, to compare type I and type II Figure 6-14
