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Measuring Biomolecular DSC Profiles with Thermolabile Ligands to Rapidly Characterize Folding and Binding Interactions
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Paisajes energéticos asociados con cambios conformacionales macromoleculares de las estructuras de punto final.

Arianna Fornili1, Barbara Giabbai, Gianpiero Garau

  • 1Biocrystallography Unit, Division of Immunology, Transplantation, and Infectious Diseases, Scientific Institute San Raffaele, Via Olgettina 58, 20132 Milan, Italy. arianna.fornili@kcl.ac.uk

Journal of the American Chemical Society
|November 19, 2010
PubMed
Resumen

Desarrollamos un nuevo método computacional para cuantificar la energía de los cambios de forma de las proteínas. Este enfoque predice con precisión la unión a las enzimas y revela cómo un solo residuo se produce.

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Área de la Ciencia:

  • Bioquímica y biología estructural.
  • Es una biofísica computacional.

Sus antecedentes:

  • La función macromolecular está modulada por cambios conformacionales, que afectan la unión de ligandos y la actividad enzimática.
  • La caracterización cuantitativa de la energética de estas dinámicas interconversiones estructurales sigue siendo un desafío debido a la falta de métodos unificados.

Objetivo del estudio:

  • Introducir un nuevo enfoque in silico para la caracterización cuantitativa de paisajes energéticos conformacionales.
  • Para permitir la investigación imparcial de reordenamientos moleculares complejos sin variables colectivas definidas por el usuario.

Principales métodos:

  • Combinación de muestreo de dinámicas esenciales y cálculos de energía libre en no equilibrio.
  • Aplicó el método para analizar cambios conformacionales en una hidrolasa de nucleósidos bacteriana.

Principales resultados:

  • Los perfiles cuantitativos de energía libre predijeron con precisión la constante de unión experimental para la enzima.
  • Demostró la naturaleza limitante de la velocidad de la transición conformacional.
  • Se identificó una inesperada función reguladora del estado de protonación de un solo residuo en la unión al sustrato y la liberación del producto.

Conclusiones:

  • El nuevo enfoque computacional proporciona un método unificado para el estudio de la energética conformacional macromolecular.
  • Esta técnica ofrece información sobre los mecanismos enzimáticos, incluida la unión al sustrato y la regulación de la liberación del producto.