Chinese Science Bulletin

, Volume 59, Issue 22, pp 2717–2725

Progress in measuring biophysical properties of membrane proteins with AFM single-molecule force spectroscopy

Progress Cell Biology

DOI: 10.1007/s11434-014-0290-x

Cite this article as:
Li, M., Liu, L., Xi, N. et al. Chin. Sci. Bull. (2014) 59: 2717. doi:10.1007/s11434-014-0290-x


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 single-molecule 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 three-dimensional structures of proteins obtained by X-ray crystallography. Here, based on the authors’ antigen-antibody 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.


Atomic force microscopy Single-molecule force spectroscopy Membrane protein Biophysical properties Biomechanics 

Copyright information

© Science China Press and Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.State Key Laboratory of Robotics, Shenyang Institute of AutomationChinese Academy of SciencesShenyangChina
  2. 2.University of Chinese Academy of SciencesBeijingChina
  3. 3.Department of Mechanical and Biomedical EngineeringCity University of Hong KongHong KongChina

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