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

TitleProgress in measuring biophysical properties of membrane proteins with AFM single-molecule force spectroscopy
Authors
KeywordsBiomechanics
Atomic force microscopy
Biophysical properties
Membrane protein
Single-molecule force spectroscopy
Issue Date2014
Citation
Chinese Science Bulletin, 2014, v. 59, n. 22, p. 2717-2725 How to Cite?
AbstractMembrane 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. © 2014 Science China Press and Springer-Verlag Berlin Heidelberg.
Persistent Identifierhttp://hdl.handle.net/10722/213415
ISSN
2015 Impact Factor: 1.789

 

DC FieldValueLanguage
dc.contributor.authorLi, Mi-
dc.contributor.authorLiu, Lianqing-
dc.contributor.authorXi, Ning-
dc.contributor.authorWang, Yuechao-
dc.date.accessioned2015-07-28T04:07:12Z-
dc.date.available2015-07-28T04:07:12Z-
dc.date.issued2014-
dc.identifier.citationChinese Science Bulletin, 2014, v. 59, n. 22, p. 2717-2725-
dc.identifier.issn1001-6538-
dc.identifier.urihttp://hdl.handle.net/10722/213415-
dc.description.abstractMembrane 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. © 2014 Science China Press and Springer-Verlag Berlin Heidelberg.-
dc.languageeng-
dc.relation.ispartofChinese Science Bulletin-
dc.subjectBiomechanics-
dc.subjectAtomic force microscopy-
dc.subjectBiophysical properties-
dc.subjectMembrane protein-
dc.subjectSingle-molecule force spectroscopy-
dc.titleProgress in measuring biophysical properties of membrane proteins with AFM single-molecule force spectroscopy-
dc.typeArticle-
dc.description.natureLink_to_subscribed_fulltext-
dc.identifier.doi10.1007/s11434-014-0290-x-
dc.identifier.scopuseid_2-s2.0-84903537705-
dc.identifier.volume59-
dc.identifier.issue22-
dc.identifier.spage2717-
dc.identifier.epage2725-
dc.identifier.eissn1861-9541-

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