title: Templates in protein de novo design.
abstract: The de novo design of polypeptide sequences with a three-dimensional structure necessary for many biological functions is limited by the complex folding process, or 'protein folding problem'. This problem can be bypassed through constructing protein-like molecules with a 'built-in' device for intramolecular folding, that is, proteins of non-natural chain architecture (template-assembled synthetic proteins, TASP). Topological templates have become a versatile tool for inducing and stabilizing secondary structures (protein loops, beta-turns, alpha-helices, beta-sheets) and are widely adopted design elements for the construction of protein-like molecules, exhibiting interesting structural and functional properties.
authors.affiliation: Institute of Organic Chemistry, University of Lausanne, Switzerland.
authors.forename: G
authors.initials: G
authors.lastname: Tuchscherer
authors.forename: M
authors.initials: M
authors.lastname: Mutter
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008958:Models, Molecular; D008961:Models, Structural; D014176:Protein Biosynthesis; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins