Circular permutation represents a form of macromolecular isomerization when the normal termini are covalently linked and new termini introduced by breaking the backbone elsewhere. Here, we describe implications of circular permutation on the folding and function of biologically relevant macromolecules. A method permitting the analysis of the folding of all circularly permuted isomers of RNA is presented that has been successfully applied for a tRNA and the binding site of the coliphage R 17 coat protein.
- Bacteriophage T4
- RNA and protein folding
- RNA-protein interactions
- circular permutation analysis
ASJC Scopus subject areas