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/
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Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation |
| title |
Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation |
| spellingShingle |
Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation Proteínas Membranas celulares Ingeniería Química |
| title_short |
Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation |
| title_full |
Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation |
| title_fullStr |
Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation |
| title_full_unstemmed |
Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation |
| title_sort |
Computational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocation |
| dc.creator.fl_str_mv |
Agudelo González, Samuel |
| dc.contributor.advisor.none.fl_str_mv |
Fernández Niño, Miguel Angel González Barrios, Andrés Fernando |
| dc.contributor.author.none.fl_str_mv |
Agudelo González, Samuel |
| dc.contributor.jury.none.fl_str_mv |
Mongui Cruz, Alvaro Cruz Jiménez, Juan Carlos |
| dc.subject.armarc.es_CO.fl_str_mv |
Proteínas Membranas celulares |
| topic |
Proteínas Membranas celulares Ingeniería Química |
| dc.subject.themes.none.fl_str_mv |
Ingeniería Química |
| description |
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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2020 |
| dc.date.issued.none.fl_str_mv |
2020 |
| dc.date.accessioned.none.fl_str_mv |
2021-02-18T12:34:43Z |
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2021-02-18T12:34:43Z |
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Trabajo de grado - Pregrado |
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http://purl.org/coar/version/c_970fb48d4fbd8a85 |
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info:eu-repo/semantics/bachelorThesis |
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http://hdl.handle.net/1992/48842 |
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u833465.pdf |
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instname:Universidad de los Andes |
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reponame:Repositorio Institucional Séneca |
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u833465.pdf instname:Universidad de los Andes reponame:Repositorio Institucional Séneca repourl:https://repositorio.uniandes.edu.co/ |
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eng |
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eng |
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http://creativecommons.org/licenses/by-nc-nd/4.0/ |
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info:eu-repo/semantics/openAccess |
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openAccess |
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18 hojas |
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application/pdf |
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Universidad de los Andes |
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Ingeniería Química Microbiología |
| dc.publisher.faculty.es_CO.fl_str_mv |
Facultad de Ingeniería Facultad de Ciencias |
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Departamento de Ingeniería Química y de Alimentos Departamento de Ciencias Biológicas |
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Al consultar y hacer uso de este recurso, está aceptando las condiciones de uso establecidas por los autores.http://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccesshttp://purl.org/coar/access_right/c_abf2Fernández Niño, Miguel Angele2a98b5e-0a6c-42ed-a315-269f52b77ab0500González Barrios, Andrés Fernandovirtual::13906-1Agudelo González, Samuelcebef1ae-9ed0-489b-9499-fb6a57123131500Mongui Cruz, AlvaroCruz Jiménez, Juan Carlos2021-02-18T12:34:43Z2021-02-18T12:34:43Z2020http://hdl.handle.net/1992/48842u833465.pdfinstname:Universidad de los Andesreponame:Repositorio Institucional Sénecarepourl:https://repositorio.uniandes.edu.co/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"Los resultados obtenidos con la OmpA como proteína que puede ser translocada en la membrana celular ha despertado el interés de identificar si existen otras proteínas que puedan ser translocadas de manera eficiente. En este estudio se analizaron dos proteínas de la membrana externa (OmpG y OmpN) por medio de un estudio in silico, para identificar si son candidatas que permitan pensar ser cargadas con el fin de liberar moléculas al interior de la célula de manera controlada. El análisis computacional permitió concluir que ambas proteínas,tienen propiedades físico-químicas que las convierten en candidatas adecuadas para ser translocadas en la membrana celular, tales como altos índices de hidrofobicidad junto a una superficie de carga que permite su adecuada interacción con el solvente y región hidrofílica de la célula. Por lo tanto, ambas proteínas fueron producidas y purificadas por medio de cromatografía de afinidad. Los resultados indican que la OmpN podría ser la proteína más adecuada para las futuras aplicaciones biomédicas debido a sus propiedades fisicoquímicas y a la cantidad de proteína que puede ser recuperada de su respectivo cultivo."--Tomado del Formato de Documento de GradoIngeniero QuímicoMicrobiólogoPregrado18 hojasapplication/pdfengUniversidad de los AndesIngeniería QuímicaMicrobiologíaFacultad de IngenieríaFacultad de CienciasDepartamento de Ingeniería Química y de AlimentosDepartamento de Ciencias Biológicasinstname:Universidad de los Andesreponame:Repositorio Institucional SénecaComputational analysis, production and purification of OmpG and OmpN as two novel protein candidates for cell membrane translocationTrabajo de grado - Pregradoinfo:eu-repo/semantics/bachelorThesishttp://purl.org/coar/resource_type/c_7a1fhttp://purl.org/coar/version/c_970fb48d4fbd8a85Texthttp://purl.org/redcol/resource_type/TPProteínasMembranas celularesIngenieríaQuímicaPublicationhttps://scholar.google.es/citations?user=xMIWHTQAAAAJvirtual::13906-10000-0003-2517-2020virtual::13906-1https://scienti.minciencias.gov.co/cvlac/visualizador/generarCurriculoCv.do?cod_rh=0000222828virtual::13906-14512efb9-3b99-4591-85f3-cfe47ddcc348virtual::13906-14512efb9-3b99-4591-85f3-cfe47ddcc348virtual::13906-1ORIGINALu833465.pdfapplication/pdf2200608https://repositorio.uniandes.edu.co/bitstreams/3ac5dd8a-fb2a-4945-8269-bc5bcf75220b/download606a3d76cf91472d68d053a6a902dde8MD51TEXTu833465.pdf.txtu833465.pdf.txtExtracted texttext/plain48296https://repositorio.uniandes.edu.co/bitstreams/a67ac7bf-0441-4cb2-bd43-0cf17f64a68e/download7c43f68fd47dcaafe1f6575343a0a0d1MD54THUMBNAILu833465.pdf.jpgu833465.pdf.jpgIM Thumbnailimage/jpeg26850https://repositorio.uniandes.edu.co/bitstreams/f3ed82aa-070d-413a-9e7d-39b925f1e337/downloade3ec4dd99f81d51f0d529d9222969d4aMD551992/48842oai:repositorio.uniandes.edu.co:1992/488422024-03-13 15:03:43.828http://creativecommons.org/licenses/by-nc-nd/4.0/open.accesshttps://repositorio.uniandes.edu.coRepositorio institucional Sénecaadminrepositorio@uniandes.edu.co |