title: How to fold intricately: using theory and experiments to unravel the properties of knotted proteins.
abstract: Over the years, advances in experimental and computational methods have helped us to understand the role of thermodynamic, kinetic and active (chaperone-aided) effects in coordinating the folding steps required to achieving a knotted native state. Here, we review such developments by paying particular attention to the complementarity of experimental and computational studies. Key open issues that could be tackled with either or both approaches are finally pointed out.
authors: Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom. Electronic address: sej13@cam.ac.uk.
authors: Sophie E
authors: SE
authors: Jackson
authors: SISSA, International School for Advanced Studies, via Bonomea 265, I-34136 Trieste, Italy.
authors: Antonio
authors: A
authors: Suma
authors: SISSA, International School for Advanced Studies, via Bonomea 265, I-34136 Trieste, Italy. Electronic address: michelet@sissa.it.
authors: Cristian
authors: C
authors: Micheletti
mesh_terms: D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins