Conformational changes in mutant lysozymes detected with monoclonal antibody
作者： Akio Kato , Toshiaki Shimizu , Shinichiro Saga
DOI: 10.1016/0014-5793(95)00846-2
关键词: Biochemistry 、 Monoclonal antibody 、 Conformational change 、 Lysozyme 、 Protein structure 、 Native state 、 Denaturation (biochemistry) 、 Chemistry 、 Mutant 、 Yeast
摘要: A monoclonal antibody (mAb) against hen egg white lysozyme (HEWL) with the exquisitely sensitive specificity to native conformation was prepared detect conformational changes in mutant lysozymes constructed by genetic modification a yeast expression system. The binding of mAb decreased both denaturation heat and guanidine-HCl, corresponding curves lysozyme. These results demonstrate that is powerful probe monitor molecule. By using this probe, change various detected. good correlation observed between ΔG (Gibbs free energy change), reflecting stability wild-type seven lysozymes. This result suggests for can be used as prove protein conformation.
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