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Unfolding and Folding Proteins

Published online by Cambridge University Press:  14 March 2018

Stephen W. Carmichael
Stephen W. Carmichael*
Affiliation:
Mayo Clinic
*
stephen.carmichael@mayo.edu

Extract

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The atomic force microscope (AFM) is being utilized in even more clever ways to reveal details of molecular structure and function. As an example, Julio Fernandez and Hongbin Li have used the AFM in the force-clamp mode to monitor the folding trajectory of a single protein. They have demonstrated in a unique way in which a single protein behaves when put under tension, and then what happens when the tension is relieved.

Fernandez and Li linked several molecules of ubiquitin, a small protein, together to form a polyubiquitin chain. With one end of the chain attached to a substrate, the tip of a soft cantilever of the AFM attached to a single protein, and from one to nine ubiquitin molecules were picked up.

Type
Research Article
Information
Microscopy Today , Volume 13 , Issue 1 , January 2005 , pp. 3 - 7
Copyright
Copyright © Microscopy Society of America 2005

Footnotes

1.

The author gratefully acknowledges Dr. Julio Fernandez for reviewing this article.

References

Notes

2. Fernandez, J.M., and H. Li, Force-clamp spectroscopy monitors the folding trajectory of a single protein, Science 303:1647-1678, 2004.