Published August 30, 2002
| public
Journal Article
A designed apoplastocyanin variant that shows reversible folding
- Creators
- Datta, Deepshikha
- Mayo, Stephen L.
Abstract
Plastocyanin, like many other metalloproteins, does not undergo reversible folding, which is thought to be due to an irreversible conformational change in the copper-binding site. Moreover, apoplastocyanin's ability to adopt a native tertiary structure is highly salt-dependent, and even in high salt, it has an irreversible thermal denaturation. Here, we report a designed apoplastocyanin variant, PCV, that is well folded and has reversible folding in both high and low salt conditions. This variant provides a tractable model for understanding and designing protein β-sheets.
Additional Information
© 2002 Elsevier Science. Received 31 July 2002; Available online 21 August 2002.Additional details
- Eprint ID
- 24077
- Resolver ID
- CaltechAUTHORS:20110620-160423337
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2011-10-03Created from EPrint's datestamp field
- Updated
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2021-11-09Created from EPrint's last_modified field