Protein structure prediction from evolutionary sequence variation (Phenylketonuria)

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Revision as of 10:12, 13 June 2013 by Waldraffs (talk | contribs) (Calculate and analyze correlated mutations)

Summary

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Multiple Sequence Alignment

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The multiple alignment of Ras (PF00071) was downloaded from Pfam.

For our protein two domains are included (ACT and Biopterin domain).

Calculate and analyze correlated mutations

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<figtable id="cn">

Ten results with highest CN for all and for extracted pairs
All pairs
pos1 aa1 pos2 aa2 MI CN
6 L 7 V 0.502378 6.00544
162 E 163 I 0.469737 5.86548
83 A 85 N 0.347723 5.55586
15 G 16 K 0.435365 4.85938
159 L 160 V 0.47458 4.82084
9 V 10 G 0.456786 4.80473
161 R 162 E 0.460369 4.63455
124 T 125 V 0.338991 4.57508
10 G 11 A 0.457641 4.51696
16 K 17 S 0.453521 4.43534
Extracted pairs
pos1 aa1 pos2 aa2 MI CN
11 A 92 D 0.324108 3.40452
81 V 116 N 0.24113 2.99935
87 T 129 Q 0.219978 2.68523
82 F 141 Y 0.246217 2.52757
84 I 115 G 0.156655 2.52503
19 L 81 V 0.14477 2.50461
82 F 115 G 0.136704 2.41712
10 G 16 K 0.39202 2.26146
130 A 141 Y 0.394896 2.24932
123 R 143 E 0.268723 2.21313
The ten results of freecontact with highest CN-value first for all pairs and second only for pairs with a distance of at least five residues. Both tables show the position of the first residue in column one with its corresponding amino acid (column 2) and of the second residue in column three with its amino acid in column four. The next one represents the mutual information score (MI) and the last one the corrected norm contact score(CN).

</figtable>

Calculate structural model

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References

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