Authors: Mi Li Lianqing Liu Ning Xi Yuechao Wang
Publish Date: 2014/04/10
Volume: 59, Issue: 22, Pages: 2717-2725
Abstract
Membrane proteins are crucial in cell physiological activities and are the targets for most drugs Thus investigating the behaviors of membrane proteins not only provide deeper insights into cell function but also help disease treatment and drug development Atomic force microscopy is a unique tool for investigating the structure of membrane proteins It can both image the morphology of single native membrane proteins with high resolution and via singlemolecule force spectroscopy SMFS directly measure their biophysical properties during molecular physiological activities such as ligand binding and protein unfolding In the context of molecular biomechanics SMFS has been successfully used to understand the structure and function of membrane proteins complementing the static threedimensional structures of proteins obtained by Xray crystallography Here based on the authors’ antigenantibody binding force measurements in clinical tumor cells the principle and method of SMFS is discussed the progress in using SMFS to characterize membrane proteins is summarized and challenges for SMFS are presented
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