title: Simplified proteins: minimalist solutions to the 'protein folding problem'.
abstract: Recent research has suggested that stable, native proteins may be encoded by simple sequences of fewer than the full set of 20 proteogenic amino acids. Studies of the ability of simple amino acid sequences to encode stable, topologically complex, native conformations and to fold to these conformations in a biologically relevant time frame have provided insights into the sequence determinants of protein structure and folding kinetics. They may also have important implications for protein design and for theories of the origins of protein synthesis itself.
authors.affiliation: Department of Biochemistry, University of Washington, Seattle 98195, USA. kwp@elina.bchem.washington.edu
authors.forename: K W
authors.initials: KW
authors.lastname: Plaxco
authors.forename: D S
authors.initials: DS
authors.lastname: Riddle
authors.forename: V
authors.initials: V
authors.lastname: Grantcharova
authors.forename: D
authors.initials: D
authors.lastname: Baker
mesh_terms: D000595:Amino Acid Sequence; D007700:Kinetics; D008958:Models, Molecular; D014176:Protein Biosynthesis; D011487:Protein Conformation; D015202:Protein Engineering; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins