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Updated: Jun 30, 2026

A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example
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Published on: May 29, 2012

Probeando las interacciones transitorias de las proteínas del chaperón de cobre y la enfermedad de Wilson a nivel de

Jaime J Benítez1, Aaron M Keller, Patrick Ochieng

  • 1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853, USA.

Journal of the American Chemical Society
|February 6, 2008
PubMed
Resumen

No abstract available in PubMed .

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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.
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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.
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