Journal
PROTEIN SCIENCE
Volume 16, Issue 7, Pages 1249-1256Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1110/ps.062673207
Keywords
protein structure/folding; conformational changes; circular dichroism; fluorescence; forces and stability; thermodynamics; hydrodynamics; kinetics; synthesis of peptides and proteins
Categories
Funding
- NIGMS NIH HHS [GM 59380, R01 GM059380] Funding Source: Medline
Ask authors/readers for more resources
Proteins adopt complex folds in nature that typically avoid conformations that are knotted or threaded'' through closed loops. Is this the result of fundamental barriers to folding, or have proteins simply evolved to avoid threaded conformations? Organic synthesis has been used in supramolecular chemistry to install topological links in small molecules. By following these principles, we now show that it is possible to assemble a topologically linked protein complex by threading a linear protein through a cyclic protein to form a [2] pseudo-rotaxane. Subsequent ring closure using native chemical ligation cyclizes the linear protein, forming a [2] heterocatenane. Although the kinetics of protein threading are slower than the folding kinetics of the native protein, threading appears to be a highly efficient process.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available