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Updated: Jun 6, 2026
07:26
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Structure and folding of a designed knotted protein
Neil P King1, Alex W Jacobitz, Michael R Sawaya
1Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095-1569, USA.
Summary
Researchers designed a novel knotted protein that successfully folds into its intended complex configuration. This study sheds light on protein folding energy landscapes and the evolution of knotted proteins.
Area of Science:
- Biochemistry
- Structural Biology
- Protein Folding
Background:
- A small fraction of natural proteins exhibit knotted configurations.
- The folding energy landscapes and evolutionary pathways of knotted proteins remain largely unexplored.
Purpose of the Study:
- To design and characterize a novel knotted protein structure.
- To investigate the folding energy landscape and evolutionary potential of designed knots.
Main Methods:
- Protein design and engineering.
- Biophysical characterization techniques.
- X-ray crystallography for structure determination.
Main Results:
- The designed protein successfully folds into the intended knotted configuration.
- The protein exhibits reversible folding kinetics.
- Folding to the native knot is significantly slower than an unknotted control protein, suggesting a complex folding pathway.
Conclusions:
- The designed protein demonstrates successful navigation of a complex folding energy landscape.
- The findings support a model for the evolution of knotted proteins through gene duplication.
- The study provides a foundation for further characterization of complex protein folding mechanisms.
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