title: Emerging principles of de novo catalyst design.
abstract: Considerable progress has been made in the understanding of how to exploit hydrophobic and charge-charge interactions in forming binding sites for peptides and small molecules in folded polypeptide catalysts. This knowledge has enabled the introduction of feedback and control functions into catalytic cycles and the construction of folded polypeptide catalysts that follow saturation kinetics. Major advances have also been made in the design of metalloproteins and metallopeptides, especially with regards to understanding redox potential control.
authors.affiliation: Department of Chemistry, Linköping University, 581 83 Linköping, Sweden. lars.baltzer@ifm.liu.se
authors.forename: L
authors.initials: L
authors.lastname: Baltzer
authors.forename: J
authors.initials: J
authors.lastname: Nilsson
mesh_terms: D001665:Binding Sites / Q000502:physiology; D002384:Catalysis; D015195:Drug Design; D005246:Feedback / Q000502:physiology; D008667:Metalloproteins / Q000737:chemistry / Q000378:metabolism*; D008670:Metals / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding
chemical_list: D008667:Metalloproteins; D008670:Metals; D010455:Peptides