title: Modelling of alpha-lactalbumin from the known structure of hen egg white lysozyme using molecular dynamics.
abstract: 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.
mesh_terms: 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
chemical_list: D007768:Lactalbumin; D009113:Muramidase; D002118:Calcium