Single-molecule force spectroscopy (SMFS) is an emerging tool to investigate mechanical properties of biomolecules and their responses to mechanical forces, and one of the most-used techniques for mechanical manipulation is the atomic force microscope (AFM). AFM was invented as an imaging tool which can be used to image biomolecules in sub-molecular resolution in physiological conditions. It can also be used as a molecular force probe for applying mechanical forces on biomolecules. In this brief review, we will provide exciting examples from recent literature which show how the advances in AFM have enabled us to gain deep insights into mechanical properties and mechanobiology of biomolecules. AFM has been applied to study mechanical properties of cells, tissues, microorganisms, viruses as well as biological macromolecules such as proteins. It has found applications in biomedical fields like cancer biology, where it has been used both in the diagnostic phases as well as drug discovery. AFM has been able to answer questions pertaining to mechanosensing by neurons, and mechanical changes in viruses during infection by the viral particles as well as the fundamental processes such as cell division. Fundamental questions related to protein folding have also been answered by SMFS like determination of energy landscape properties of variety of proteins and their correlation with their biological functions. A multipronged approach is needed to diversify the research, as a combination with optical spectroscopy and computer-based steered molecular dynamic simulations along with SMFS can help us gain further insights into the field of biophysics and modern biology.
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Tohoku Univ, Grad Sch Engn, Dept Mat Proc, Aoba Ku, Sendai, Miyagi 9808579, JapanTohoku Univ, Grad Sch Engn, Dept Mat Proc, Aoba Ku, Sendai, Miyagi 9808579, Japan
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Univ South Dakota, Dept Biomed Engn, Sioux Falls, SD 57104 USA
BioSNTR, Sioux Falls, SD 57104 USAUniv South Dakota, Dept Biomed Engn, Sioux Falls, SD 57104 USA
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Pohang Univ Sci & Technol, Dept Chem, Pohang 790784, South KoreaPohang Univ Sci & Technol, Dept Chem, Pohang 790784, South Korea
Kim, Jung Sook
Park, Yu Shin
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DGIST, Ctr Core Res Facil, Taegu 711873, South KoreaPohang Univ Sci & Technol, Dept Chem, Pohang 790784, South Korea
Park, Yu Shin
Nam, Hong Gil
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Ctr Plant Aging Res, Inst Basic Sci, Taegu 711873, South Korea
DGIST, Dept New Biol, Taegu 711873, South KoreaPohang Univ Sci & Technol, Dept Chem, Pohang 790784, South Korea
Nam, Hong Gil
Park, Joon Won
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Pohang Univ Sci & Technol, Dept Chem, Pohang 790784, South KoreaPohang Univ Sci & Technol, Dept Chem, Pohang 790784, South Korea
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Chinese Acad Sci, Shenyang Inst Automat, State Key Lab Robot, Shenyang 110016, Liaoning, Peoples R ChinaChinese Acad Sci, Shenyang Inst Automat, State Key Lab Robot, Shenyang 110016, Liaoning, Peoples R China
Li Mi
Xi Ning
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Chinese Acad Sci, Shenyang Inst Automat, State Key Lab Robot, Shenyang 110016, Liaoning, Peoples R China
Univ Hong Kong, Dept Ind & Mfg Syst Engn, Hong Kong, Hong Kong, Peoples R ChinaChinese Acad Sci, Shenyang Inst Automat, State Key Lab Robot, Shenyang 110016, Liaoning, Peoples R China
Xi Ning
Wang Yue-Chao
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Chinese Acad Sci, Shenyang Inst Automat, State Key Lab Robot, Shenyang 110016, Liaoning, Peoples R ChinaChinese Acad Sci, Shenyang Inst Automat, State Key Lab Robot, Shenyang 110016, Liaoning, Peoples R China
Wang Yue-Chao
Liu Lian-Qing
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Chinese Acad Sci, Shenyang Inst Automat, State Key Lab Robot, Shenyang 110016, Liaoning, Peoples R ChinaChinese Acad Sci, Shenyang Inst Automat, State Key Lab Robot, Shenyang 110016, Liaoning, Peoples R China