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Videos de Conceptos Relacionados

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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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.
The...
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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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Protein Folding01:25

Protein Folding

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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...
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Protein Folding01:22

Protein Folding

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Protein Folding01:22

Protein Folding

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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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An isotype-specific phosphorylation of Hsp90 rewires co-chaperone regulations.

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Association-induced folding governs surrogate light chain and pre-B cell receptor core assembly.

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The essential co-chaperone Sgt1 regulates client dwell time in the Hsp90 chaperone cycle.

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Video Experimental Relacionado

Updated: Apr 2, 2026

Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors
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Malachite Green Assay for the Discovery of Heat-Shock Protein 90 Inhibitors

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hsp90: torcer y doblar y doblar.

Klaus Richter1, Johannes Buchner

  • 1Department of Chemistry, Technische Universität München, Germany.

Cell
|October 24, 2006
PubMed
Resumen

Los acompañantes moleculares como la proteína de choque térmico 90 (Hsp90) ayudan al plegamiento de las proteínas. Nuevas estructuras cristalinas iluminan el ciclo de reacción Hsp90, revelando su mecanismo para la maduración de la proteína cliente.

Área de la Ciencia:

  • La bioquímica es la bioquímica.
  • Biología Molecular Biología Molecular
  • Biología Estructural Biología estructural.

Sus antecedentes:

  • Las chaperonas moleculares son maquinaria celular esencial responsable del plegamiento de las proteínas, previniendo la agregación y facilitando la función adecuada de las proteínas.
  • Las proteínas de choque térmico, particularmente Hsp90, juegan un papel crítico en las respuestas de estrés celular y la regulación de diversas vías de señalización mediante la estabilización de las proteínas cliente.

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