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Ultrafast folding kinetics of WW domains reveal how the amino acid sequence determines the speed limit to protein folding by Malwina Szczepaniak; Manuel Iglesias-Bexiga; Michele Cerminara; Mourad Sadqi; Celia Sanchez de Medina; Jose C. Martinez; Irene Luque; Victor Muñoz is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.
What is Ultrafast folding kinetics of WW domains reveal how the amino acid sequence determines the speed limit to protein folding about?
Protein (un)folding rates depend on the free-energy barrier separating the native and unfolded states and a prefactor term, which sets the timescale for crossing such barrier or folding speed limit. Because extricating these two factors is usually unfeasible, it has been common to assume a constant prefactor and assign all rate variability to the barrier. However, theory and simulations postulate a protein-specific prefactor that contains key mechanistic information. Here, we exploit the special properties of fast-folding proteins to experimentally resolve the folding rate prefactor and investigate how much it varies among structural homologs. We measure the ultrafast (un)folding kinetics of five natural WW domains using nanosecond laser-induced temperature jumps. All five WW domains fold in microseconds, but with a 10-fold difference between fastest and slowest. Interestingly, they all produce biphasic kinetics in which the slower phase corresponds to reequilibration over the small barrier (<3 ) and the faster phase to the downhill relaxation of the minor population residing at the barrier top [transition state ensemble (TSE)]. The fast rate recapitulates the 10-fold range, demons
Who reads Ultrafast folding kinetics of WW domains reveal how the amino acid sequence determines the speed limit to protein folding?
It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.
- Author
- Malwina Szczepaniak; Manuel Iglesias-Bexiga; Michele Cerminara; Mourad Sadqi; Celia Sanchez de Medina; Jose C. Martinez; Irene Luque; Victor Muñoz
- Publisher
- National Academy of Sciences; Proceedings of the National Academy of Sciences; Oxford University Press (OUP); Publons; ScienceOpen (ISSN 0027-8424)
- Published
- 2019
- Language
- EN
- Field
- Biochemistry, Genetics and Molecular Biology (Life Sciences)