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...

Full description

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/
Description
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