Difference between revisions of "Part:BBa K1640024:Experience"
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| − | + | IngenuityLab_Canada 2016 | |
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| − | + | Nafaa Haddou | |
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| − | + | As part of our gold medal requirement we further characterizes a pre-existing BioBrick in the registry. Part BBa_K1640024 was modeled using SwissModel to show the tertiary structure. The ribbon model was rendered using multiple templates of other highly characterized CP47 protein crystals found through Protein Data Bank. The sequences were aligned using the BLAST and the SwissModel script. Secondary structures were assigned based on homology and the alignment with the templates. Closer alignment allowed for better estimation of the structure. The secondary structures were then used to stack the image and develop the tertiary structure. Finally, energy minimization was done to render the most stable orientation and organization of the amino sequence in tertiary form. | |
| − | + | The model allows for a better understanding of how the protein interacts within the complex since function is derived from structure. The secondary structures also allow for comparison and identification of key domains and motifs that are necessary for protein function. Likewise these regions are usually conserved and thus the can be used in the identification of unknown functions or the characterization of similar proteins in the organism as well as others. | |
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| − | + | [[File:Team Ingenuity Lab CP43.png]] | |
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Revision as of 04:41, 26 October 2016
This experience page is provided so that any user may enter their experience using this part.
Please enter
how you used this part and how it worked out.
Applications of BBa_K1640024
User Reviews
UNIQ97aee20dd4ef9a4b-partinfo-00000000-QINU IngenuityLab_Canada 2016
Nafaa Haddou
As part of our gold medal requirement we further characterizes a pre-existing BioBrick in the registry. Part BBa_K1640024 was modeled using SwissModel to show the tertiary structure. The ribbon model was rendered using multiple templates of other highly characterized CP47 protein crystals found through Protein Data Bank. The sequences were aligned using the BLAST and the SwissModel script. Secondary structures were assigned based on homology and the alignment with the templates. Closer alignment allowed for better estimation of the structure. The secondary structures were then used to stack the image and develop the tertiary structure. Finally, energy minimization was done to render the most stable orientation and organization of the amino sequence in tertiary form. The model allows for a better understanding of how the protein interacts within the complex since function is derived from structure. The secondary structures also allow for comparison and identification of key domains and motifs that are necessary for protein function. Likewise these regions are usually conserved and thus the can be used in the identification of unknown functions or the characterization of similar proteins in the organism as well as others.
UNIQ97aee20dd4ef9a4b-partinfo-00000001-QINU