抄録
The whey protein β-Lactoglobulin has been investigated in aqueous solution (pH 7, 298.15 K) by molecular dynamic simulation up to pressures of 650 MPa for short process times. Results reveal for dimers a pressure dependent compressibility of 0.15 GPa-1 (50...200 MPa) and 0.11 GPa-1 (250...650 MPa), which agrees well with literature data. Compressibilities of helices, strands, loops and cavities show different values. These are related to the specific protein architecture of β-lactoglobulin. For pressures greater than 350 MPa, the compressibility of the protein core decreases significantly due to penetration of water into the molecule. The analysis of relative movement of the two monomers indicates that the dissociation process starts with a rotation.
