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At room temperature, the chair conformer of cyclohexane undergoes rapid ring flipping between two equivalent chair conformers at a rate of approximately 105 times per second. These two chair conformers are in equilibrium. The rapid ring flipping results in the interconversion of the axial proton to an equatorial proton and an equatorial to the axial proton. Such interconversions are too rapid and cannot be detected on the NMR timescale. Hence, the NMR spectrometer cannot distinguish between the...
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Aromatic compounds can be identified or analyzed using proton NMR and carbon‐13 NMR. Typically, aromatic hydrogens or hydrogens directly bonded to the aromatic rings are strongly deshielded by the aromatic ring current. Therefore, they absorb in the range of 6.5–8.0 ppm in proton NMR spectra. For instance, aromatic hydrogens directly bonded to the benzene ring absorb at 7.3 ppm. However, aromatic hydrogens of larger rings absorb farther upfield or downfield than the ideal range.
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The axial and equatorial protons in cyclohexane can be distinguished by performing a variable-temperature NMR experiment. In this process, except for one proton, the remaining eleven protons are replaced by deuterium. The deuterium substitution avoids the possible peak splitting caused by the spin-spin coupling between the adjacent protons. The remaining proton flips between the axial and equatorial positions.
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Different notations are used to represent the three-dimensional structure of molecules on two-dimensional surfaces. One of the most commonly used representations is the dash-wedge formula. The dashed wedges, solid wedges, and the plane lines indicate the groups situated behind the plane, coming out of the plane, and in the plane, respectively.
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Visualización de los movimientos respiratorios de proteínas asociados con el giro del anillo aromático

Laura Mariño Pérez1,2, Francesco S Ielasi3, Luiza M Bessa1

  • 1Université Grenoble Alpes, CEA, CNRS, IBS, Grenoble, France.

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Las cadenas laterales aromáticas de proteínas pueden rotar, lo que requiere que se rodeen

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Área de la Ciencia:

  • Biología estructural
  • Dinámica de las proteínas
  • La bioquímica

Sus antecedentes:

  • Los residuos aromáticos son cruciales para la estabilidad del núcleo de la proteína.
  • Los estudios de resonancia magnética nuclear (RMN) indicaron que las cadenas laterales aromáticas pueden girar (voltear anillos) dentro de las proteínas.
  • Se planteó la hipótesis de que los movimientos de "respiración" de las proteínas facilitaban estos giros de anillo, pero faltaban detalles estructurales.

Objetivo del estudio:

  • Para dilucidar las reorganizaciones estructurales que acompañan el cambio de anillo de un residuo de tirosina enterrado en un dominio SH3.
  • Proporcionar información estructural de alta resolución sobre los movimientos de respiración de las proteínas asociados con la dinámica de la cadena lateral.

Principales métodos:

  • Se utilizó la espectroscopia de RMN para observar el cambio de la cadena lateral de tirosina.
  • Se realizó un análisis de secuencias proteomáticas para diseñar mutantes estabilizadores.
  • Se empleó la cristalografía de rayos X para determinar la estructura de alta resolución del estado menor.

Principales resultados:

  • Demostró que las transiciones de la cadena lateral de tirosina a un estado menor de baja población.
  • Identificó la generación de volumen vacío alrededor del anillo de tirosina durante la transición.
  • Capturado la estructura de alta resolución del estado menor estabilizado.

Conclusiones:

  • El estudio revela la base estructural de los movimientos de respiración de proteínas que permiten el cambio de anillo de la cadena lateral aromática.
  • Los hallazgos ofrecen información sobre la interacción entre el entorno proteico local y las conformaciones de la cadena lateral de aminoácidos.
  • Los resultados tienen implicaciones para el diseño de proteínas y la predicción de la estructura.