Statistical Mechanical Model for pH-Induced Protein Folding: Application to Apomyoglobin

• DOI: 10.1021/acs.jpcb.6b06936
• Publication Date: 2016-08-05T02:28:17Z
• Authors: Takuya Mizukami; Yosuke Sakuma; Kosuke Maki
• Keywords: Folding (DSP implementation)

Despite the major role of pH in protein folding and stability, a quantitative understanding pH-induced mechanism remains elusive. Two conventional models, Monod-Wyman-Changeux Linderstrøm-Lang smeared charge respectively, have been used to analyze formation/disruption specific native structures fluctuating non-native states. However, there are only few models that can represent overall kinetic events folding/unfolding independent properties relevant molecular species, which has hampered efforts systematically folding. Here, we constructed statistical mechanical model incorporates protonation along with combined manual search least-squares fitting procedure, was investigate horse apomyoglobin over wide range (2.2-6.7), time window ranging from ∼40 μs ∼100 s, using continuous-/stopped-flow fluorescence at 8 °C. Quantitative analysis assuming five-state sequential scheme indicated (1) is represented by both binding Coulombic interactions; (2) intermediates share mechanisms equilibrium intermediate, indicating their equivalence; (3) native-like acquired successively during transition This could also be applied variety association/dissociation processes.