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T-wave Ion Mobility-mass Spectrometry: Basic Experimental Procedures for Protein Complex Analysis
Published on: July 31, 2010
La estructura cristalina del carbono monoxi-mioglobina fotolisado tiene una estructura cristalina
I Schlichting1, J Berendzen, G N Phillips
1Department of Biophysics, Max Planck Institute for Medical Research, Heidelberg, Germany.
Nature
|October 27, 1994
Resumen
La fotodisociación de carbono-monoxi-mioglobina (MbCO) utilizando la luz crea un intermediario inestable. La cristalografía de rayos X reveló el CO CO.
Área de la Ciencia:
- La biofísica es la biofísica.
- Biología Estructural Biología estructural.
- Dinámica de las proteínas Dinámica de las proteínas.
Sus antecedentes:
- La mioglobina (Mb) es una proteína clave que se une al oxígeno.
- El monóxido de carbono-mioglobina (MbCO) es un sistema modelo para el estudio de las reacciones de las proteínas.
- La fotodisociación de MbCO libera CO, formando un intermediario transitorio.
Objetivo del estudio:
- Para determinar la estructura del intermediario inestable MbCO.
- Para aclarar los cambios estructurales que acompañan a la fotodisociación de CO en la mioglobina.
Principales métodos:
- Cristalografía de rayos X a temperaturas de helio líquido.
- Determinación estructural de alta resolución (1.5 Å).
Principales resultados:
- El CO fotodisociado se localizó por encima del anillo pirrólico de hemo C.
- Los cambios estructurales incluyen el 'doming' del hemo, el desplazamiento del hierro, la compresión del enlace proximal de histidina, la tensión de la hélice F y el reposicionamiento distal de la histidina.
Conclusiones:
- El estudio proporciona una instantánea de alta resolución del intermediario MbCO.
- Revela importantes reorganizaciones estructurales de las proteínas tras la fotodisociación del ligando.
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