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Dinámica lenta de las redes de triptófano-agua en las proteínas

R Bryn Fenwick¹, David Oyen¹, H Jane Dyson¹

¹The Scripps Research Institute , 10550 North Torrey Pines Road, La Jolla, California 92037, United States.

Journal of the American Chemical Society

|December 20, 2017

Resumen

La dinámica del agua unida a las proteínas influye en la función biomolecular. Los estudios de RMN revelan cambios en la geometría de la red de agua durante los cambios de conformación de las proteínas, que afectan a los procesos biológicos.

Área de la Ciencia:

La bioquímica
Biología estructural
La biofísica

Sus antecedentes:

El agua influye significativamente en la dinámica biomolecular y los procesos biológicos.
Los cambios conformacionales de las proteínas en escalas de tiempo de microsegundos a milisegundos (μs-ms) están relacionados con la función de las proteínas.
El comportamiento del agua unida a las proteínas durante estos cambios conformacionales funcionales sigue siendo poco comprendido.

Objetivo del estudio:

Investigar el papel y la dinámica del agua unida a las proteínas durante los cambios conformacionales funcionales.
Para sondear la dinámica de la red de agua indirectamente mediante mediciones de dispersión de relajación por RMN.
Comprender cómo el agua media la comunicación entre las regiones proteicas durante los cambios conformacionales.

Principales métodos:

Se utilizaron mediciones de dispersión de relajación por RMN para estudiar los indoles de triptófano en la dihidrofolato reductasa (DHFR).
Cambios de desplazamiento químico analizados de los protones del indole NH y de los átomos de nitrógeno del anillo durante los cambios estructurales en la escala de tiempo μs-ms.
Cambios químicos experimentales integrados con predicciones de la teoría funcional de la densidad (DFT).

Principales resultados:

Se observaron cambios químicos significativos en los protones de indole NH, pero cambios más pequeños en los nitrógenos de anillo durante las transiciones estructurales.
Demostró que los protones de triptófano indole NH permanecen unidos al agua, mientras que la geometría de la red de agua circundante cambia.
Se estableció que la dispersión de relajación puede informar indirectamente sobre la dinámica del agua.

Conclusiones:

La geometría del agua unida a las proteínas cambia dinámicamente durante los cambios conformacionales de las proteínas μs-ms.
Las moléculas de agua juegan un papel crítico en la transmisión de información a través de regiones de proteínas funcionalmente importantes.
Los movimientos internos de la proteína pueden acoplarse a través de redes de agua enlazadas con hidrógeno dentro de la estructura de la proteína.

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