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A Liquid Phase Affinity Capture Assay Using Magnetic Beads to Study Protein-Protein Interaction: The Poliovirus-Nanobody Example
Published on: May 29, 2012
Probing transient copper chaperone-Wilson disease protein interactions at the single-molecule level with nanovesicle
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
Abstract
No abstract available in PubMed .
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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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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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