Rs121907967

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Revision as of 16:39, 23 June 2011 by Uskat (talk | contribs)

Pysicochemical Properities

Trp TER consequences
aromatic, polar, hydrophobic TER By this change, the protein is not complete, therefore it is not possible for the protein to fold and to function.

Visualisation of the Mutation

picture original aa picture mutated aa combined picture
Amino acid Tryptophan
Visualization of the mutated protein

Subsitution Matrices Values

PAM 1 Pam 250 BLOSOUM 62
value aa most frequent substitution rarest substitution value aa most frequent substitution rarest substitution value aa most frequent substitution rarest substitution
X 2 (Arg) 0 (all, except Arg, Phe, Ser, Tyr) X 2 (Arg) 0 (all, except Arg, His, Leu, Phe, Ser, Tyr) X 2 (Tyr) -4 (Asn, Asp, Pro)

Conservation Analysis with Multiple Alignments

Mutation in the multiple alignment

=== Secondary Structure Mutation Analysis

JPred:
...CCCCCCCCCCCCHHHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHHCCCEEEEECC...
PsiPred:
...CCCCCCCCCCCCHHHHHHHHHCCCCCCHHHHHHHHHHHHHHHHHHCCCCEEEECC...

Comparison with the real structure:

Mutation at position 329
Mutation at position 329 - detailed view

SNAP Prediction

No prediction available, because the protein ends here.

A detailed list of all possible substitutions can be found [here]


SIFT Prediction

SIFT Matrix:
Each entry contains the score at a particular position (row) for an amino acid substitution (column). Substitutions predicted to be intolerant are highlighted in red.

Sift legend.png
329 sift.png.png




PolyPhen2 Prediction

HumDiv prediction
HumVar prediction