TY - JOUR
T1 - Theory of nanobubble formation and induced force in nanochannels
AU - Arai, Noriyoshi
AU - Koishi, Takahiro
AU - Ebisuzaki, Toshikazu
N1 - Funding Information:
This work was supported by JSPS KAKENHI Grants No. JP26106006 and JP17K14610.
Publisher Copyright:
© 2017 American Physical Society.
PY - 2017/10/11
Y1 - 2017/10/11
N2 - This paper presents a fundamental theory of nanobubble formation and induced force in confined nanochannels. It is shown that nanobubble formation between hydrophobic plates can be predicted from their surface tension and geometry, with estimated values for the surface free energy and the force acting on the plates in good agreement with the results of molecular dynamics simulation and experimentation. When a bubble is formed between two plates, vertical attractive force and horizontal retract force due to the shifted plates are applied to the plates. The net force exerted on the plates is not dependent on the distance between them. The short-range force between hydrophobic surfaces due to hydrophobic interaction appears to correspond to the force estimated by our theory. We compared between experimental and theoretical values for the binding energy of a molecular motor system to validate our theory. The tendency that the binding energy increases as the size of the protein increases is consistent with the theory.
AB - This paper presents a fundamental theory of nanobubble formation and induced force in confined nanochannels. It is shown that nanobubble formation between hydrophobic plates can be predicted from their surface tension and geometry, with estimated values for the surface free energy and the force acting on the plates in good agreement with the results of molecular dynamics simulation and experimentation. When a bubble is formed between two plates, vertical attractive force and horizontal retract force due to the shifted plates are applied to the plates. The net force exerted on the plates is not dependent on the distance between them. The short-range force between hydrophobic surfaces due to hydrophobic interaction appears to correspond to the force estimated by our theory. We compared between experimental and theoretical values for the binding energy of a molecular motor system to validate our theory. The tendency that the binding energy increases as the size of the protein increases is consistent with the theory.
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U2 - 10.1103/PhysRevE.96.042802
DO - 10.1103/PhysRevE.96.042802
M3 - Article
C2 - 29347539
AN - SCOPUS:85032857657
SN - 1063-651X
VL - 96
JO - Physical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics
JF - Physical Review E - Statistical Physics, Plasmas, Fluids, and Related Interdisciplinary Topics
IS - 4
M1 - 042802
ER -