Article
Allostery in the ferredoxin protein motif does not involve a conformational switch.
Proceedings of the National Academy of Sciences of the United States of America - 8 Feb 2011
Nechushtai Rachel, Lammert Heiko, Michaeli Dorit, Eisenberg-Domovich Yael, Zuris John A, Luca Maria A, Capraro Dominique T, Fish Alex, Shimshon Odelia, Roy Melinda, Schug Alexander, Whitford Paul C, Livnah Oded, Onuchic José N, Jennings Patricia A
Abstract excerpt
Regulation of protein function via cracking, or local unfolding and refolding of substructures, is becoming a widely recognized mechanism of functional control. Oftentimes, cracking events are localized to secondary and tertiary structure interactions between domains that control the optimal position for catalysis and/or the formation of protein complexes. Small changes in free energy associated with ligand...
Topics
- Allosteric Regulation
- Amino Acid Motifs
- Ferredoxins
- Humans
- Iron
- Models, Molecular
- Mutation
- Protein Folding
- Protein Stability
- Protein Structure, Tertiary