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Kyoto University Uematsu Lab
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A lab that uses physics to unravel the mysteries of bubbles, droplets, ions, and biomolecules.

AboutAbout the lab
Solving the mysteries of bubbles and droplets with physics
The Soft Matter Physics Division (Uematsu Lab) aims to understand chemical and biological phenomena as physics through liquids and soft matter.
The lab conducts both measurement experiments using light, electric fields, and flow, and theory based on thermodynamics, statistical mechanics, and fluid dynamics.
Its main themes are the physics of bubbles and droplets, ion-specific effects on biomolecules, and unsolved problems in chemical physics and biophysics.
Key terms
- Soft matter
- Soft materials that deform easily, such as polymers, colloids, liquid crystals, and foams
- Ion-specific effects
- A phenomenon in which the behavior of a material changes depending on the type of ion, even when the charge is the same
- Contact angle
- The angle formed between the edge of a droplet and the surface when the droplet rests on a solid surface
NewsLab news
A paper by Associate Professor Uematsu and colleagues was published in NEXT MATERIALS
A paper by Associate Professor Uematsu and colleagues was published in The Journal of Chemical Physics
A paper by Associate Professor Uematsu and colleagues was published in Physica A: Statistical Mechanics and its Applications
A paper by Associate Professor Uematsu and colleagues was published in The Journal of Physical Chemistry C
ResearchResearch themes
Building on measurement experiments using light, electric fields, and flow fields, together with theoretical analysis based on thermodynamics, statistical mechanics, and fluid dynamics, the lab aims to discover new physical phenomena involving interfaces, ions, and biomolecules and to elucidate their mechanisms.
*Illustrative imageThe physics of bubbles and droplets
In recent years, the stability and functions of micro- to nanoscale bubbles have attracted attention. Together with the behavior of droplet contact angles and contact lines, the lab studies interfacial problems from the viewpoint of physics.
*Illustrative imageIon-specific effects on biomolecules
Proteins are charged macromolecules, and the way they disperse in solution changes when salt is added. Using experimental methods from light scattering and colloid chemistry, the lab investigates how changes in shape and charge depending on the type of ion are linked to biological function.
*Illustrative imageUnsolved problems in chemical physics and biophysics
The lab pursues research out of interest in effects such as chemical reactions being accelerated in tiny water droplets, isotope effects of water in soft matter, and the ion selectivity of nanochannels such as ion channels.
MembersFaculty
- Associate ProfessorYuki Uematsu
VoicesStudent voices
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Report an errorAbout the images
The top and research theme images are illustrative and were not taken at the lab. They are cropped from Wikimedia Commons images. Cropped CC BY-SA images are provided under the same CC BY-SA license as the original (version shown on each line).
- Top image: “Cluster of sea foam bubbles on Muriwai Beach” Avenue / CC BY-SA 3.0 (cropped)
- The physics of bubbles and droplets: “Water droplets on steel surface (2016)” akshatsgi / CC BY-SA 4.0 (cropped)
- Ion-specific effects on biomolecules: “Cryo-EM structure of human CPSF160-WDR33-CPSF30-CPSF100 PIM complex - 6URG” Zhang Y, Sun Y, Shi Y, Walz T, Tong L / CC0 (cropped)
- Unsolved problems in chemical physics and biophysics: “Water droplet lying on a damask” Petar Milošević / CC BY-SA 4.0 (cropped)
- Related lab (Active Matter Lab): “DNA Origami Triangular” Matthias A. Fenner / CC BY-SA 4.0 (cropped)
- Related lab (Condensed Matter Physics Lab): “FQHE Hall” Jakubtr / CC BY-SA 3.0 (cropped)
- Related lab (Plant Molecular Genetics Lab (comprising the Inagaki, Takenaka, and Tsugeki Groups)): “Confocal microscopy with spectral imaging- Five-color observation of organelles in Marchantia polymorpha thallus cells ( )” ZEISS Microscopy from Germany / CC BY-SA 2.0 (cropped)
- Related lab (Biological Structural Chemistry Lab): “Glycine and glutamate bound Human GluN1a-GluN2D NMDA receptor - Glutamate receptor ionotropic, NMDA 1 - 8E96” Chou, T.-H., Furukawa, H. / CC0 (cropped)
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