title: Transmuting alpha helices and beta sheets.
abstract: Protein architecture involves two main secondary structural classes: alpha helices and beta sheets. Some natural proteins alter their fold in response to changes in solution conditions or as a consequence of mutation. Here, we discuss recent attempts to induce such conformational changes by design: specifically, the motivation and success of efforts to change one protein fold into a different one in response to the 'Paracelsus Challenge'. The results of such efforts may provide a better understanding of the processes that underlie conformational plasticity in proteins.
authors.affiliation: Department of Chemistry, Yale University, New Haven, CT 06520, USA.
authors.forename: S
authors.initials: S
authors.lastname: Dalal
authors.forename: S
authors.initials: S
authors.lastname: Balasubramanian
authors.forename: L
authors.initials: L
authors.lastname: Regan
mesh_terms: D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins / Q000737:chemistry; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D015202:Protein Engineering; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry; D016601:RNA-Binding Proteins / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry
chemical_list: D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; C106926:Janus protein, Bacteria; D010455:Peptides; D011506:Proteins; D016601:RNA-Binding Proteins; D011994:Recombinant Proteins; C108906:crotein G; C038154:paracelsin