17 April 2017 Single molecule dynamics of polyproline by using AFM
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Abstract
Polyproline forms a unique structure, called polyproline helix. It takes polyproline II helix in water and Polyproline I helix in n-propanol. PP II is known to be a rigid molecule in spite of no hydrogen bonds between backbone atoms, and to play an important role in biological functions such as formation of collagen structure and in the cell-adhesion. In this study, we carried out single molecule force spectroscopy of polyproline with AFM(Atomic Force Microscope) and covalent immobilization of polyproline molecule on gold substrate to evaluate the rigidity of PP II at single molecule level. We found that the force-extension curve of polyproline shows a linear increase, which is unusual and not seen with others homo-polypeptide molecules. These results indicate that the high rigidity of polyproline II helix can be explained by “enthalpic”, not “entropic” driven elasticity.
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Hironori Tamamushi, Masaru Kawakami, Hidemitsu Furukawa, "Single molecule dynamics of polyproline by using AFM", Proc. SPIE 10167, Nanosensors, Biosensors, Info-Tech Sensors and 3D Systems 2017, 101671R (17 April 2017); doi: 10.1117/12.2257629; https://doi.org/10.1117/12.2257629
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