Descripción físico-química teórica y computacional de los complejos enzima-ligando de la proteína bromelina reportada mediante difracción de Rayos X

Fabián Mauricio Santana Romo; Marcia Jimena Morales Ortíz; Aurora Lisette Carreño Otero; Gabriela Elena Vizuete Fiallos; Jessica Lorena Peñaherrera Veintimilla

doi:10.33789/talentos.11.1.193

Fabián Mauricio Santana Romo Universidad de las Fuerzas Armadas https://orcid.org/0000-0002-8753-3349
Marcia Jimena Morales Ortíz Universidad de las Fuerzas Armadas https://orcid.org/0000-0002-2711-6391
Aurora Lisette Carreño Otero Investigador independiente https://orcid.org/0000-0003-2357-4798
Gabriela Elena Vizuete Fiallos Universidad de las Fuerzas Armadas https://orcid.org/0009-0000-0593-6527
Jessica Lorena Peñaherrera Veintimilla Universidad de las Fuerzas Armadas https://orcid.org/0009-0009-0732-9494

DOI: https://doi.org/10.33789/talentos.11.1.193

Palabras clave: Bromelina, cristalografía, enzima-ligando, físico-química, proteína, Rayos X

Resumen

El estudio teórico computacional aborda la descripción de los complejos enzima-ligando obtenidos mediante el método de difracción de Rayos X. El propósito de este estudio es analizar a la enzima bromelina aplicando de la química computacional, a través de cribados virtuales consecutivos en la plataforma del RCSB PDB hasta llegar al cristal de mejor calidad reportada. La descripción física de la obtención de coordenadas tridimensionales a través del modelo de difracción de Rayos X, y la aplicación de la química teórica y computacional para describir la proteína cuaternaria reportada con sus cadenas, ligandos asociados, y moléculas de agua estructural. Se determinó que el complejo cristalino ID PDB: 6YCB es el que posee la mejor resolución, comparándola con respecto a la proteína en criogenia que minimiza sus vibraciones estructurales.

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