Intricate Knots in Proteins: Function and Evolution
By Peter Virnau, Leonid A. Mirny, Mehran Kardar. PLoS Comput. Biol., 2006
342 citations recorded by the source corpus.
Our investigation of knotted structures in the Protein Data Bank reveals the most complicated knot discovered to date. We suggest that the occurrence of this knot in a human ubiquitin hydrolase might be related to the role of the enzyme in protein degradation. While knots are usually preserved among homologues, we also identify an exception in a transcarbamylase. This allows us to exemplify the function of knots in proteins and to suggest how they may have been created.
Subfields: Genetics, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/e76d9c54288b509d4fc03d6458faf96565a7f30b
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
In Genetics
In Molecular Biology
- Cristian Micheletti
- William R. Taylor
- Leonid A. Mirny
- Enzo Orlandini
- Davide Marenduzzo
- Santo Fortunato
- Réka Albert
Citations in the corpus
- Protein knots and fold complexity: Some new twists (2007, background): “Virnau et al. (2006) provided a survey of the known knots in he protein databank, of which there are now almost 40.”
- Protein knot server: detection of knots in protein structures (2007, methodology): “Note that unlike in our previous work (11), PDB residue numbers are used to describe the location of the knots.”
- Polymers with spatial or topological constraints: Theoretical and computational results (2011, background): “A very high consistency exists among the different methods of closure regarding the knotted/unknotted state of individual protein chains and also regarding the occurring types of knots [36, 37, 38, 39, 40, 41, 42, 35].”