Metalloprotein Folding
Abstract
One of the most intriguing problems in the biological sciences is the question of how to predict protein structure and function based on knowledge of a gene sequence. While significant progress has been made toward this goal during the past decade, fundamental challenges remain, such as understanding important post-translational modifications. One of the most critical post-translational modifications is the incorporation of a metal or metal cofactor into a catalytic or structural site in order to gain proper function. At the same time, some proteins function solely to recognize, transport, or sequester metals. When we consider how metals affect protein structure and function, we should not neglect their role in protein folding and stability as well as their participation in protein dynamics, as all are essential for optimal activity. Thus, workers in bioinorganic chemistry have an opportunity to be major contributors to the fields of protein folding and structure prediction.
Additional Information
© 2004 American Chemical Society. Received November 3, 2004. Publication Date (Web): December 6, 2004.Additional details
- Eprint ID
- 76721
- DOI
- 10.1021/ic040121q
- Resolver ID
- CaltechAUTHORS:20170419-154018328
- Created
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2017-04-19Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field