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dc.titleDynamics of hydrogen nanobubbles in KLH protein solution studied with in situ wet-TEM
dc.contributor.authorHuang, T.-W.
dc.contributor.authorLiu, S.-Y.
dc.contributor.authorChuang, Y.-J.
dc.contributor.authorHsieh, H.-Y.
dc.contributor.authorTsai, C.-Y.
dc.contributor.authorWu, W.-J.
dc.contributor.authorTsai, C.-T.
dc.contributor.authorMirsaidov, U.
dc.contributor.authorMatsudaira, P.
dc.contributor.authorChang, C.-S.
dc.contributor.authorTseng, F.-G.
dc.contributor.authorChen, F.-R.
dc.identifier.citationHuang, T.-W., Liu, S.-Y., Chuang, Y.-J., Hsieh, H.-Y., Tsai, C.-Y., Wu, W.-J., Tsai, C.-T., Mirsaidov, U., Matsudaira, P., Chang, C.-S., Tseng, F.-G., Chen, F.-R. (2013-10-07). Dynamics of hydrogen nanobubbles in KLH protein solution studied with in situ wet-TEM. Soft Matter 9 (37) : 8856-8861. ScholarBank@NUS Repository.
dc.description.abstractAlthough the stability of the nanobubble remains a controversial issue that is subject to the classical predictions of high Laplace pressure, we demonstrate that a hydrogen nanobubble can be generated and stabilized in an aqueous solution of Keyhole limpet hemocyanin (KLH) protein via an electron radiolysis process. The hydrogen gas inside the nanobubble is in a "dense gas" phase that is characterized by a Knudsen number and number density of hydrogen molecules. The dynamics of nanobubbles are analyzed using time-series electron microscopy images. The growth of small nanobubbles will be affected by the largest neighboring nanobubble; however, a diffusive shielding effect for small nanobubbles is observed. Locally, anti-Ostwald ripening of nanobubbles can be observed; however, the global growth behavior among the nanobubbles is randomly correlated because the characteristic diffusion length of the hydrogen molecules is considerably greater than the average spacing among the nanobubbles. © 2013 The Royal Society of Chemistry.
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.sourcetitleSoft Matter
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