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Protein Structure

In order to better understand the structural conservation between aligned molecules, certain tools involving the coloring of molecules are used within MultiSeq. In particular, Q per residue measures structure conservation. Structure conservation occurs when the structures between aligned proteins are similar.

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\begin{minipage}{.2\textwidth}
\includegraphics[width=2...
...ontribution from each residue to the overall average Q value.}
\end{minipage} }

Q per residue, is accessed by:

1 Click on the View menu on the MultiSeq window.
2 Select Molecule Coloring.
Figure 7: Molecule Coloring
Molecule Coloring



When you select Molecule Coloring another side menu should appear with the following options: Q per residue and Sequence Identity per residue.


Select Q per residue to visualize structural conservation. Look at the OpenGL Display window to see the impact this selection has made on the molecules.
 

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...? What does this mean in terms of the evolution of the AARSs?}
\end{minipage} }


Figure 8: Structure Conservation
Structure Conservation
 


You will probably notice that several portions within the interior of the aligned molecules have turned blue. Rotate the molecule to see how much of it has turned blue. The blue areas indicate that the molecules are structurally conserved at those points. The red regions are not structurally conserved, and these correspond to insertions, which are typically found on the periphery of the molecule as shown in Figure 7 of O'Donoghue et al.


 
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\begin{minipage}{.2\textwidth}
\includegraphics[width=2...
...nds with what you highlighted in the {\sf Sequence Display}. }
\end{minipage} }


next up previous contents
Next: Protein Sequence Up: Comparing Protein Structure And Previous: Comparing Protein Structure And   Contents
Brijeet Dhaliwal 2004-09-15