Modelling of alpha-lactalbumin from the known structure of hen egg white lysozyme using molecular dynamics.
The prediction of protein conformation by homology is being widely pursued using interactive computer graphics. However, there have been a limited number of energy minimization and/or molecular dynamics studies for such predictions. This paper reports one such study on alpha-lactalbumin, a system that can be tested as the X-ray crystal structure has recently been determined. The differences in structure of the Ca2+ binding loop reported for the holo-protein (Stuart et al., Nature, 324 [1986] 84-87) and that predicted for the apoprotein could be attributed to the presence or absence of the Ca2+ ion.
D000818:Animals; D001665:Binding Sites; D002118:Calcium; D002645:Chickens; D003198:Computer Simulation; D006801:Humans; D007768:Lactalbumin; D008958:Models, Molecular; D009113:Muramidase; D011487:Protein Conformation; D013816:Thermodynamics; D014961:X-Ray Diffraction
D007768:Lactalbumin; D009113:Muramidase; D002118:Calcium