Article
Complex Folding Landscape of Apomyoglobin at Acidic pH Revealed by Ultrafast Kinetic Analysis of Core Mutants.
The journal of physical chemistry. B - 13 Dec 2018
Mizukami Takuya, Xu Ming, Fazlieva Ruzaliya, Bychkova Valentina E, Roder Heinrich
Abstract excerpt
Under mildly acidic conditions (pH 4-4.5) apomyoglobin (apoMb) adopts a partially structured equilibrium state ( M-state) that structurally resembles a kinetic intermediate encountered at a late stage of folding to the native structure at neutral pH. We have previously reported that the M-state is formed rapidly (<1 ms) via a multistate process and thus offers a unique opportunity for exploring early stages of...
Topics
- Animals
- Apoproteins
- Hydrogen-Ion Concentration
- Hydrophobic and Hydrophilic Interactions
- Kinetics
- Mutagenesis, Site-Directed
- Mutation
- Myoglobin
- Protein Conformation, alpha-Helical
- Protein Unfolding
- Sperm Whale
- Thermodynamics