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Videos de Conceptos Relacionados

Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding01:22

Protein Folding

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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Amyloid Fibrils03:03

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Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Microfluidic Mixers for Studying Protein Folding
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Published on: April 10, 2012

Cómo se pliegan las proteínas de rápido plegamiento.

Kresten Lindorff-Larsen1, Stefano Piana, Ron O Dror

  • 1D. E. Shaw Research, New York, NY 10036, USA. kresten.lindorff-larsen@DEShawResearch.com

Science (New York, N.Y.)
|October 29, 2011
PubMed
Resumen
Este resumen es generado por máquina.

Comprender el plegamiento de las proteínas es clave en la biología molecular. Las simulaciones revelan principios comunes para diversas proteínas que se pliegan espontáneamente en estructuras nativas a través de vías predecibles.

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Área de la Ciencia:

  • Biología Molecular Biología Molecular
  • La biofísica es la biofísica.
  • Biología computacional Biología computacional.

Sus antecedentes:

  • El plegamiento de proteínas en estructuras tridimensionales es un proceso fundamental en la biología molecular.
  • Comprender los principios que rigen el plegamiento de las proteínas sigue siendo un desafío científico significativo.

Objetivo del estudio:

  • Investigar los principios comunes que subyacen al plegamiento de las proteínas.
  • Para simular el plegamiento espontáneo de diversas proteínas utilizando detalles a nivel atómico.

Principales métodos:

  • Se realizaron simulaciones de dinámica molecular a nivel atómico.
  • Las simulaciones oscilaron entre 100 microsegundos y 1 milisegundo.
  • Se empleó una sola función de energía basada en la física.

Principales resultados:

  • 12 proteínas estructuralmente diversas se plegaron espontáneamente y repetidamente a sus estructuras nativas.
  • La columna vertebral de la proteína adoptó una topología similar a la nativa al principio del plegamiento.
  • Las vías de plegado a menudo estaban dominadas por una sola ruta, correlacionada con la propensión a los residuos.

Conclusiones:

  • Los principios comunes rigen el plegamiento de proteínas estructuralmente diversas.
  • Las simulaciones demuestran la capacidad de los modelos basados en la física para recapitular el plegamiento de las proteínas.
  • El orden de la formación de elementos durante el plegado es predecible y está vinculado al estado desplegado.