Abstract
The bovine dairy protein β-lactoglobulin (βlg) is a promiscuous protein that has the ability to bind several hydrophobic ligands. In this study, based on known experimental data, the dynamic interaction mechanism between bovine βlg and four fatty acids was investigated by a protocol combining molecular dynamics (MD) simulations and molecular mechanics generalized Born surface area (MMGBSA) binding free energy calculations. Energetic analyses revealed binding free energy trends that corroborated known experimental findings; larger ligand size corresponded to greater binding affinity. Finally, binding free energy decomposition provided detailed information about the key residues stabilizing the complex.
Original language | English |
---|---|
Pages (from-to) | 1010-1018 |
Number of pages | 9 |
Journal | Biopolymers |
Volume | 101 |
Issue number | 10 |
DOIs | |
State | Published - Oct 2014 |
Keywords
- capric acid
- caprylic acid
- free energy calculation
- lactoglobulin
- molecular dynamics
- myristic acid
- stearic acid