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La desnaturalización en frío de la proteína como se ve desde el disolvente.

Monika Davidovic1, Carlos Mattea, Johan Qvist

  • 1Department of Biophysical Chemistry, Center for Molecular Protein Science, Lund University, SE-22100 Lund, Sweden.

Journal of the American Chemical Society
|January 1, 2009
PubMed
Resumen

Se investigó la desnaturalización en frío de las proteínas globulares utilizando la relajación de espín de agua-{17) O. Sólo la apomioglobina desestabilizada se desnaturalizó en frío, desafiando las suposiciones comunes sobre las interacciones proteína-agua y los mecanismos de desnaturalización en frío.

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Área de la Ciencia:

  • La biofísica es la biofísica.
  • Dinámica de las proteínas Dinámica de las proteínas.
  • La termodinámica es la termodinámica.

Sus antecedentes:

  • Las proteínas globulares tienen una temperatura de máxima estabilidad, a diferencia de la mayoría de los sistemas ordenados.
  • La desnaturalización en frío, o alteración de la estructura por enfriamiento, está típicamente relacionada con las fuerzas hidrofóbicas.
  • Falta la investigación experimental de los cambios de hidratación durante la desnaturalización en frío.

Objetivo del estudio:

  • Para monitorear experimentalmente la dinámica de hidratación de las proteínas a bajas temperaturas.
  • Para investigar los fenómenos de desnaturalización en frío en varias proteínas globulares.
  • Comprender el papel de las interacciones proteína-agua en la desnaturalización en frío.

Principales métodos:

  • Se utilizó la relajación del espín del agua-(17) O para estudiar la dinámica de la hidratación.
  • Se estudiaron las proteínas (BPTI, ubiquitina, apomioglobina, beta-lactoglobulina) en una solución acuosa.
  • Las soluciones estaban contenidas en picolitros de gotas de emulsión para evitar la formación de hielo hasta -35°C.

Principales resultados:

  • Sólo la apomioglobina desestabilizada exhibió desnaturalización en frío.
  • La ubiquitina se mantuvo estable hasta -32°C; la beta-lactoglobulina fue inestable por debajo de -5°C pero cinéticamente atrapada.
  • Los estados desnaturalizados en frío eran compactos y penetrados por disolventes, no totalmente desplegados, lo que desafió las analogías con la solubilidad de moléculas no polares.

Conclusiones:

  • La desnaturalización en frío es específica de las proteínas e influenciada por la estabilidad y la hidratación.
  • Los estados de desnaturalización en frío observados sugieren una penetración del disolvente en lugar de un despliegue completo.
  • La denaturación fría reportada en algunos sistemas puede deberse a un bajo contenido de agua, no solo a la temperatura.