Helical peptide and protein design.
The design of dimeric coiled-coils has ultimately led to novel applications, such as self-replicating peptide systems, whereas the structural features of the less common trimeric coiled-coil continue to be elucidated. Novel topologies have been discovered in designed proteins, as exemplified by the right-handed tetrameric coiled-coil and the inverted U four-helix bundle, and a single switch of two amino acids within a protein has been shown to be sufficient to designate a new protein fold. Conformational switching from helix to sheet has been observed for designed peptides and transcription factors, whereas peptides designed from beta-amino acids have been found to adopt a helical conformation in aqueous solution.
Micklatcher
C
C
Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
Chmielewski
J
J
D000595:Amino Acid Sequence; D015195:Drug Design; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011506:Proteins / Q000138:chemical synthesis / Q000737:chemistry*
D010455:Peptides; D011506:Proteins