Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation
The results obtained with the OmpA as a protein that can be translocated in cell membrane has caused interest in identifying if there are other proteins that could be translocated in a more efficient way. In this study two outer membrane proteins (OmpG and OmpN) were analyzed in silico to identify i...
- Autores:
-
Agudelo González, Samuel
- Tipo de recurso:
- Trabajo de grado de pregrado
- Fecha de publicación:
- 2020
- Institución:
- Universidad de los Andes
- Repositorio:
- Séneca: repositorio Uniandes
- Idioma:
- eng
- OAI Identifier:
- oai:repositorio.uniandes.edu.co:1992/48842
- Acceso en línea:
- http://hdl.handle.net/1992/48842
- Palabra clave:
- Proteínas
Membranas celulares
Ingeniería
Química
- Rights
- openAccess
- License
- http://creativecommons.org/licenses/by-nc-nd/4.0/
Summary: | The results obtained with the OmpA as a protein that can be translocated in cell membrane has caused interest in identifying if there are other proteins that could be translocated in a more efficient way. In this study two outer membrane proteins (OmpG and OmpN) were analyzed in silico to identify if one of they could be a proper candidate for being translocated in the membrane. Computational analysis of both proteins pointed out that they have physicochemical properties that make them proper candidates for being translocated in cell membrane as high levels of hydrophobicity and the charge surface. Therefore, they were produced and purified by affinity between a histidine tag and an immobilized metal in magnetic beads. Finally, the results indicate that OmpN could be the protein that might be more suited for future biomedical applications of the porins |
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