Molecular simulation of partially denatured β-lactoglobulin

The unfolding of β-lactoglobulin (β-lac) upon heating was comprehensively studied through molecular dynamics computer simulations. A β-lac molecule in the aqueous solution firstly heated at 500 K for and then annealed 300 to collect stable conformations. There were five meta-stable conformations observed based on Free Energy Landscape (FEL). found exhibit an open extended conformation followed by limited refolding cooling. cysteine residues –SH121 S–S66-160 most located opposite ends molecule. This would favour intermolecular –SH/S–S interchange reactions that are known occur as part inter-molecular aggregation process. Furthermore, increased hydrogen bond forming capacity between water molecules protein themselves. interactions properties hydration shell also indicated stabilized unfolding. However, it diffusion molecules, including those first interact more strongly with protein. may partly explain why unfolded proteins likely aggregate even though there protecting them. Such results provided detailed information structure-functionality relationship both its shell. provides insight into how we can control processing desirable functional such thickening gelation, which modified protein-water interactions.