Difference between revisions of "Rs61731240"
(→Conservation analysis with multiple alignments)
(→Secondary structure mutation analysis)
|Line 65:||Line 65:|
=== Secondary ===
Revision as of 17:56, 23 June 2011
|aromatic, positive charged, polar, hydrophilic||negative charged, small, polar, hydrophilic||On the one side, both amino acids are polar, but on the other side, His is positively charged, while Asp is negatively charged, which is an essential difference between these both amino acids. Therefore it is very likely, that this change causes big changes in the structure of the protein and the protein therefore will probably not work any longer. Furthermore, the structure of the two amino acids is very different, because of the aromatic ring of the His.|
Visualisation of the Mutation
|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|
|3||20 (Gln)||0 (Ile, Met)||4||7 (Gln)||2 (Ala, Cys, Gly, Ile, Leu, Met, Phe, Thr, Trp, Val)||-1||2 (Tyr)||-3 (Cys, Ile, Leu, Val)|
Conservation analysis with Multiple Alignments
Secondary Structure Mutation Analysis
JPred: ...EEEECCCCCEEEEEECCCCCCCHHHHHHHHHHHHHHCCCEEEEEEECCCCCCCCC... PsiPred: ...EEECCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHCCCCEEEEEECCCCCCCEEC...
Comparison with the real structure:
|Substitution||Prediction||Reliability Index||Expected Accuracy|
A detailed list of all possible substitutions can be found [here]
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.
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.