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Thermodynamics of Membrane Protein Folding Measured by Fluorescence Spectroscopy
Published on: April 28, 2011
Influencia de la fluoración en la termodinámica del plegamiento de las proteínas
Benjamin C Buer1, Benjamin J Levin, E Neil G Marsh
1Departments of †Chemistry and ‡Biological Chemistry, University of Michigan , Ann Arbor, Michigan 48109, United States.
Journal of the American Chemical Society
|July 18, 2012
Resumen
La adición de aminoácidos fluorados mejora la estabilidad de las proteínas. Este estudio revela la base termodinámica, mostrando que el aumento de la estabilidad se debe principalmente a cambios desfavorables en la entropía, no en la entalpía, vinculados a los efectos hidrofóbicos.
Área de la Ciencia:
- La ingeniería de proteínas es la ingeniería de proteínas.
- Química biofísica es la química biofísica.
- La termodinámica es la termodinámica.
Sus antecedentes:
- Los aminoácidos altamente fluorados aumentan la estabilidad de las proteínas contra el calor y los denaturantes.
- Los fundamentos termodinámicos de este efecto de estabilización aún no se comprenden completamente.
Objetivo del estudio:
- Investigar la base termodinámica (entálpica vs. entrópica) de la estabilidad proteica mejorada en las proteínas fluoradas.
- Para correlacionar la termodinámica desplegada con el contenido de flúor y la superficie accesible al disolvente.
Principales métodos:
- Parámetros termodinámicos determinados (ΔH°, ΔS°, ΔCp°) para el despliegue de 12 proteínas de nuevo diseño.
- Variada composición de núcleo hidrofóbico con residuos fluorados y no fluorados.
- Cambios calculados en el área de superficie accesible al disolvente apolar.
Principales resultados:
- El aumento del contenido de flúor se correlacionó con una mayor energía libre de despliegue, impulsada por cambios desfavorables de entropía (ΔS°).
- Capacidad térmica de despliegue positiva (ΔCp°) correlacionada con el área de superficie accesible al disolvente apolar.
- La entalpia de despliegue (ΔH°) no mostró correlación con el contenido de flúor o la superficie.
Conclusiones:
- Los efectos hidrofóbicos convencionales explican suficientemente la estabilidad mejorada de la mayoría de las proteínas altamente fluoradas.
- La excepcional estabilidad térmica de estas proteínas se debe en parte a una muy baja capacidad térmica por residuo (ΔCp°), similar a las proteínas termostables naturales.
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