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Conservación de la dinámica de la cadena lateral dentro de una familia de proteínas
Anthony B Law1, Ernesto J Fuentes, Andrew L Lee
1Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, USA.
Journal of the American Chemical Society
|April 21, 2009
Resumen
La dinámica de la cadena lateral de las proteínas se conserva sorprendentemente, incluso en parientes lejanos de las proteínas. Esta flexibilidad conservada, vinculada al plegamiento global de la proteína, puede ser crucial para la función de la proteína.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Estructural Biología estructural.
- La biofísica es la biofísica.
Sus antecedentes:
- La dinámica de las proteínas es crítica para la función biológica.
- Los movimientos de la cadena lateral ocurren en escalas de tiempo de picosegundos a nanosegundos.
- Comprender la dinámica de las proteínas ayuda en el diseño de fármacos y la ingeniería de proteínas.
Objetivo del estudio:
- Para comparar el movimiento de la cadena lateral monitoreado por RMN en tres dominios de ZPD.
- Para investigar la conservación de la dinámica de la cadena lateral de las proteínas.
- Para determinar si la dinámica de las proteínas se puede predecir a partir de la secuencia o la estructura.
Principales métodos:
- Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN) Espectroscopía de Resonancia Magnética Nuclear (RMN).
- Mediciones de relajación del metilo (2) H. Mediciones de relajación del metilo (2) H.
- Cálculo de los parámetros de orden de la cadena lateral (S(2)).
Principales resultados:
- La dinámica de la cadena lateral mostró una conservación significativa en los dominios de PDZ con identidad de secuencia baja.
- Las dinámicas observadas fueron más similares a las predichas por la secuencia o el embalaje local.
- La dinámica de las proteínas se predijo mejor con proteínas homólogas que con los métodos actuales basados en la estructura.
Conclusiones:
- Las dinámicas rápidas de la cadena lateral están organizadas y vinculadas al plegamiento global de la proteína.
- Las interacciones no locales y los movimientos correlacionados influyen en la flexibilidad de la cadena lateral.
- La dinámica proteica conservada probablemente juega un papel directo en la función de las proteínas.
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