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Microfluidic Mixers for Studying Protein Folding
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Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

Protein folding rates correlate with heterogeneity of folding mechanism

B Oztop1, M R Ejtehadi, S S Plotkin

  • 1Department of Physics and Astronomy, University of British Columbia, Vancouver, BC V6T-1Z1, Canada.

Physical Review Letters
|December 17, 2004
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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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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