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Updated: Jun 29, 2026

Microfluidic Mixers for Studying Protein Folding
12:42

Microfluidic Mixers for Studying Protein Folding

Published on: April 10, 2012

探测蛋白质类折叠稳定性的下限尺寸:在水中具有特定的刚性结构的十余微蛋白

Brandon L Kier1, Niels H Andersen

  • 1Department of Chemistry, University of Washington, Seattle, Washington 98195, USA.

Journal of the American Chemical Society
|October 10, 2008
PubMed
概括

研究人员通过优化特定相互作用来设计稳定,短的系统. 这些新的"微蛋白"在水中有效折叠,显示最小的运动和高化温度.

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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.
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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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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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