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Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

What lessons can be learned from studying the folding of homologous proteins?

Adrian A Nickson1, Jane Clarke

  • 1University of Cambridge, Department of Chemistry, MRC Centre for Protein Engineering, Lensfield Road, Cambridge CB2 1EW, UK.

Methods (San Diego, Calif.)
|June 24, 2010
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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Conservation of Protein Domains Over Different Proteins

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