Unfolding the Mysteries of Protein Metamorphosis. ACS Chem Biol 2018 Jun 15;13(6):1438-1446
Date
05/23/2018Pubmed ID
29787234Pubmed Central ID
PMC6007232DOI
10.1021/acschembio.8b00276Scopus ID
2-s2.0-85047568358 (requires institutional sign-in at Scopus site) 60 CitationsAbstract
Since the proposal of Anfinsen's thermodynamic hypothesis in 1963, our understanding of protein folding and dynamics has gained significant appreciation of its nuance and complexity. Intrinsically disordered proteins, chameleonic sequences, morpheeins, and metamorphic proteins have broadened the protein folding paradigm. Here, we discuss noncanonical protein folding patterns, with an emphasis on metamorphic proteins, and we review known metamorphic proteins that occur naturally and that have been engineered in the laboratory. Finally, we discuss research areas surrounding metamorphic proteins that are primed for future exploration, including evolution, drug discovery, and the quest for previously unrecognized metamorphs. As we enter an age where we are capable of complex bioinformatic searches and de novo protein design, we are primed to search for previously unrecognized metamorphic proteins and to design our own metamorphs to act as targeted, switchable drugs; biosensors; and more.
Author List
Dishman AF, Volkman BFAuthor
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
AnimalsBacteria
Humans
Intrinsically Disordered Proteins
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Engineering
Protein Folding
Protein Unfolding