Team:UPO-Sevilla/Foundational Advances/MiniTn7/Bioinformatics/Whole phylogeny

From 2011.igem.org

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                             <h1>Results. Analysis throughout the whole phylogeny</h1>
                             <h1>Results. Analysis throughout the whole phylogeny</h1>
                              
                              
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<p>Previously to the study of the codifying nucleotide glmS sequences, Glms protein was analyzed to check the reported high level of conservation of the C-terminal part of this protein (Milewski, 2002) (http://www.sciencedirect.com/science/article/pii/S0167483802003187). Thus, a multialignment, a circular and squared tree and several logos of all the downloaded Glms sequences were obtained (figure 5). It is mentionable the high level of conservation found in the last 15 amino acids of this protein in all organisms which contrast with the lack of any conservation in the previous amino acidic sequence (this difference is perfectly shown in all sequence logos). It is also interesting that the consensus sequence of this C-terminal part of Glms protein match perfectly with the amino acidic sequence resulting when translating the nucleotide consensus obtained in figure 3.</p>
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<p>Previously to the study of the codifying nucleotide glmS sequences, Glms protein was analyzed to check the reported high level of conservation of the C-terminal part of this protein (<a href="http://www.sciencedirect.com/science/article/pii/S0167483802003187" target="_blank">Milewski, 2002</a>). Thus, a multialignment, a circular and squared tree and several logos of all the downloaded Glms sequences were obtained (figure 5). It is mentionable the high level of conservation found in the last 15 amino acids of this protein in all organisms which contrast with the lack of any conservation in the previous amino acidic sequence (this difference is perfectly shown in all sequence logos). It is also interesting that the consensus sequence of this C-terminal part of Glms protein match perfectly with the amino acidic sequence resulting when translating the nucleotide consensus obtained in figure 3.</p>
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<img class="center" width="300px" src="https://static.igem.org/mediawiki/2011/9/91/UPOSevilla-BioInfo-Fig5.jpg" alt="Glms protein multi-sequence alignment"/>
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<p><strong>Figure 5</strong>. Glms protein multi-sequence alignment</p>
                         </div>
                         </div>

Revision as of 16:31, 19 September 2011

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Results. Analysis throughout the whole phylogeny

Previously to the study of the codifying nucleotide glmS sequences, Glms protein was analyzed to check the reported high level of conservation of the C-terminal part of this protein (Milewski, 2002). Thus, a multialignment, a circular and squared tree and several logos of all the downloaded Glms sequences were obtained (figure 5). It is mentionable the high level of conservation found in the last 15 amino acids of this protein in all organisms which contrast with the lack of any conservation in the previous amino acidic sequence (this difference is perfectly shown in all sequence logos). It is also interesting that the consensus sequence of this C-terminal part of Glms protein match perfectly with the amino acidic sequence resulting when translating the nucleotide consensus obtained in figure 3.

Glms protein multi-sequence alignment

Figure 5. Glms protein multi-sequence alignment

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