Difference between revisions of "Rs1800430"
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=== Visualisation of the Mutation === |
=== Visualisation of the Mutation === |
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+ | In the next step, we created the visualization of the muation with PyMol. Therefore we created a picture for the original amino acid, for the new mutated amino acid and finally for both together in one picture whereas the mutation is white colored. The following pictures display that the mutated amino acid Asparagine looks very different to Aspartic acid. They both agree in the first part of the rest but then go complety in opposite directions. Otherwise both rests fork at the end. All in all, the different directions prevail and will therefore probably cause big structural changes which will cause effects on the protein function. |
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Revision as of 20:14, 25 June 2011
Contents
General Information
SNP-id | rs1800430 |
Codon | 399 |
Mutation Codon | Asn -> Asp |
Mutation Triplet | AAC -> GAC |
Pysicochemical Properities
First of all, we explored the amino acid properties and compared them for the original and the mutated amino acid. Therefore we created the possible effect that the mutation could have on the protein.
Asn | Asp | consequences |
polar, small, hydrophilic, negatively charged | polar, small, hydrophilic, negatively charged | Both amino acids have the same properities and therefore we suggest that an exchange of these two amino acids do not destroy the protein structure and function |
Visualisation of the Mutation
In the next step, we created the visualization of the muation with PyMol. Therefore we created a picture for the original amino acid, for the new mutated amino acid and finally for both together in one picture whereas the mutation is white colored. The following pictures display that the mutated amino acid Asparagine looks very different to Aspartic acid. They both agree in the first part of the rest but then go complety in opposite directions. Otherwise both rests fork at the end. All in all, the different directions prevail and will therefore probably cause big structural changes which will cause effects on the protein function.
picture original aa | picture mutated aa | combined picture |
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 |
36 | 36 (Asp) | 0 (Cys, Met) | 7 | 7 (Asp) | 2 (Cys, Leu, Phe, Trp) | 1 | 1 (Asp, His, Ser) | -4 (Trp) |
PSSM analysis
self-information | expected self-information | |
Asn | 0 | 5 |
Asp | 0 | 4 |
Conservation Analysis with Multiple Alignments
Secondary Structure Mutation Analysis
JPred: ...CCCCCCCEEEEEECCCCCCCCHHHHHHHHHCCCCEEECCCCCCCCCCCCCCCCCC... PsiPred: ...CCCCCCCCEEEEECCCCCCCHHHHHHHHHHCCCEEEECCCCCCCCCCCCCCCCCC...
Comparison with the real structure:
SNAP Prediction
Substitution | Prediction | Reliability Index | Expected Accuracy |
D | Neutral | 1 | 60% |
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 Table
Threshold for intolerance is 0.05.
Amino acid color code: nonpolar, uncharged polar, basic, acidic.
Capital letters indicate amino acids appearing in the alignment, lower case letters result from prediction.
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