Difference between revisions of "Team:IIT Madras/Results"

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<div style="text-align:center"><img height="350px" width="350px" src="https://static.igem.org/mediawiki/2015/7/7a/Alyteserin_structural_feature.png">  
 
<div style="text-align:center"><img height="350px" width="350px" src="https://static.igem.org/mediawiki/2015/7/7a/Alyteserin_structural_feature.png">  
<img height="350px" width="350px" src = "https://static.igem.org/mediawiki/2015/7/72/Naly_structural_feature.png"></div>
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<img height="350px" width="350px" src = "https://static.igem.org/mediawiki/2015/7/72/Naly_structural_feature.png"></div><figcaption><b>Fig :<b>Structural features of Alyteserin-1a, aa sequence GLKDIFKAGLGSLVKGIAAHVAN and Naly, aa sequecne IAGYAEEILEHVIAE</figcaption>
  
 
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<h2>Analyzing MD Simulation Results</h2>
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<div style="text-align:center"><img src="https://static.igem.org/mediawiki/2015/3/36/Distance_peptide_complex_iitm.png"></div><figcaption>Distance between both the peptides over time in MD simulations.</figcaption><br></br>
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<div style="text-align:center"><img src = "https://static.igem.org/mediawiki/2015/a/a4/Vaccum_energy_of_peptides_iitm.png"></div><figcaption>Total energy of the system in vaccum over time in MD simulations.</figcaption><br></br>
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<div style="text-align:center"><img src = "https://static.igem.org/mediawiki/2015/c/ce/Gyr_largepep_iitm.png"></div><figcaption>Radius of gyration of Alyteserin-1a, antimicrobial peptide, over time in MD simulations.</figcaption><br></br>
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<div style="text-align:center"><img src = "https://static.igem.org/mediawiki/2015/e/e7/Gyr_smallpep_iitm.png"></div><figcaption>Radius of gyration of Naly, neutralizing antimicrobial peptide, over time in MD simulations.</figcaption><br></br>
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<h2>GROMACS Simulation</h2>
 
<h2>GROMACS Simulation</h2>
 
<div style="text-align:center"><img height="372px" width="650px" src = "https://static.igem.org/mediawiki/2015/0/05/Igem.gif"></div>
 
<div style="text-align:center"><img height="372px" width="650px" src = "https://static.igem.org/mediawiki/2015/0/05/Igem.gif"></div>

Revision as of 05:01, 18 September 2015

in silico


Predicting structure of a neutralising protein

To achieve our goal of achieving an antimicrobial free environment, it was necessary to inactivate the antimicrobial peptide Alyteserin. When a protein interacts with another protein, its structure is altered. This prevents the protein from performing from it's usual function. This was what we set out to do-design a small peptide that would interact with Alyteserin favourably under specified conditions. We also tried to simulate the interaction between the two peptides using GROMACS, and the results will be discussed later on on this page. First let's analyse the structure of Alyteserin.

Structural Features of Alyteserin and Naly

Fig :Structural features of Alyteserin-1a, aa sequence GLKDIFKAGLGSLVKGIAAHVAN and Naly, aa sequecne IAGYAEEILEHVIAE


Interactions



Analyzing MD Simulation Results

Distance between both the peptides over time in MD simulations.


Total energy of the system in vaccum over time in MD simulations.


Radius of gyration of Alyteserin-1a, antimicrobial peptide, over time in MD simulations.


Radius of gyration of Naly, neutralizing antimicrobial peptide, over time in MD simulations.




GROMACS Simulation

Molecular Dynamics Simulation of the interactions between Alyteserin(red) and NAly(green)