Difference between revisions of "Talk:Fabry:Sequence alignments (sequence searches and multiple alignments)"
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Rackersederj (talk | contribs) |
Rackersederj (talk | contribs) |
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# whole structure of our Task2 wiki pages was changed :) |
# whole structure of our Task2 wiki pages was changed :) |
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# => you are right! This problem needs to be fixed. Thanks! --[[User:Rackersederj|Rackersederj]] 08:20, 7 May 2012 (UTC) |
# => you are right! This problem needs to be fixed. Thanks! --[[User:Rackersederj|Rackersederj]] 08:20, 7 May 2012 (UTC) |
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| − | => fixed --[[User:Rackersederj|Rackersederj]] 11:38, 7 May 2012 (UTC) |
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| + | : => Problem is fixed. Now all identifiers are considered. The results are also compared to the results where only one ID is considered. --[[User:Rackersederj|Rackersederj]] 13:12, 7 May 2012 (UTC) |
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| + | TODO: |
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| + | Maybe only interesting parts or the active site...? --[[User:Rackersederj|Rackersederj]] 13:07, 5 May 2012 (UTC) ... Active site (D170 and D231) and partly the surrounding parts are highly conserved! Functional sites... maybe also Glycosylation site (139,192,215,408) and Disulfide bonds (52 ↔ 94, 56 ↔ 63, 142 ↔ 172, 202 ↔ 223, 378 ↔ 382) |
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Latest revision as of 16:34, 7 May 2012
Some quick feedback (still at work):
- I would change the Task2 link on your main page to this one (results) instead of the other one that looks like the protocol --Bernhoferm 12:02, 6 May 2012 (UTC)
- How do you compare HHblits with Blast? It looks like you took only one protein per cluster from HHblits (or are your clusters so small?) and compared it to the results from Blast.
- whole structure of our Task2 wiki pages was changed :)
- => you are right! This problem needs to be fixed. Thanks! --Rackersederj 08:20, 7 May 2012 (UTC)
- => Problem is fixed. Now all identifiers are considered. The results are also compared to the results where only one ID is considered. --Rackersederj 13:12, 7 May 2012 (UTC)
TODO: Maybe only interesting parts or the active site...? --Rackersederj 13:07, 5 May 2012 (UTC) ... Active site (D170 and D231) and partly the surrounding parts are highly conserved! Functional sites... maybe also Glycosylation site (139,192,215,408) and Disulfide bonds (52 ↔ 94, 56 ↔ 63, 142 ↔ 172, 202 ↔ 223, 378 ↔ 382)
