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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy
Published on: September 17, 2017
Correlación entre los parámetros de orden de la cadena lateral de RMN 2H y la conservación de la secuencia en
Anthony Mittermaier1, Alan R Davidson, Lewis E Kay
1Protein Engineering Network Centres of Excellence, University of Toronto, Toronto, Ontario, Canada M5S 1A8.
Journal of the American Chemical Society
|September 17, 2004
Resumen
La preferencia de la secuencia de proteínas, no solo la accesibilidad al disolvente, influye en la movilidad de la cadena lateral en las proteínas. Las características estructurales conservadas, como los enlaces de hidrógeno, parecen gobernar la dinámica interna de las proteínas.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Estructural Biología estructural.
- La biofísica es la biofísica.
Sus antecedentes:
- La dinámica de las cadenas laterales es crucial para la función de las proteínas.
- El enterramiento hidrofóbico es un factor conocido que influye en la dinámica interna de las proteínas.
- La comprensión de los factores que rigen la dinámica interna de las proteínas es clave para la ingeniería de proteínas y el diseño de fármacos.
Objetivo del estudio:
- Para investigar la relación entre la preferencia de la secuencia, la accesibilidad del disolvente y la dinámica de la cadena lateral en las proteínas.
- Identificar las características estructurales conservadas que dictan la dinámica interna de las proteínas más allá de las interacciones hidrofóbicas.
Principales métodos:
- Se recogieron datos de relajación de RMN 2H de cadena lateral para el dominio SH3 de la tirosina quinasa Fyn.
- Se analizaron los datos de relajación con respecto a la preferencia de la secuencia y la accesibilidad del disolvente por residuo.
- Se compararon los hallazgos en seis sistemas de proteínas adicionales.
Principales resultados:
- Los residuos con mayor preferencia de secuencia mostraron una movilidad reducida en comparación con el promedio.
- La preferencia por la secuencia mostró una correlación más fuerte con la movilidad que con la accesibilidad al solvente.
- Esta tendencia fue consistente en la mayoría de las proteínas estudiadas.
- Identificó enlaces de hidrógeno de cadena lateral y estructuras secundarias específicas como determinantes potenciales de la dinámica interna.
Conclusiones:
- La preferencia de secuencia es un determinante significativo de la movilidad de la cadena lateral en las proteínas.
- Las características estructurales conservadas, incluidos los enlaces de hidrógeno y las estructuras secundarias, juegan un papel vital en el gobierno de la dinámica interna de las proteínas.
- Estos hallazgos ofrecen nuevos conocimientos sobre los principios de las relaciones estructura-función de las proteínas.
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