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Biomolecular Chemistry Lab
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The lab measures microparticles one by one and also investigates how hemoglobin works.
AboutAbout the lab
Studying microparticles one by one to uncover how hemoglobin works
The Biomolecular Chemistry Lab studies the physical and chemical processes that occur at the interfaces and inside of tiny particles and droplets, as well as the mechanism by which cooperativity arises in hemoglobin.
In its microparticle research, the lab traps and manipulates a single microparticle under a microscope using laser light or a microcapillary, and examines it with electrochemical and spectroscopic measurements.
For hemoglobin, the lab investigates how cooperativity arises as oxygen binds.
The lab's website still shows the name "Nakatani Lab," but the lab started as the Nagatomo Lab in April 2026.
Key terms
- Single microparticle
- Individual microparticles that are trapped and measured one by one under a microscope, rather than as an average over many
- Hemoglobin
- A heme protein in red blood cells that carries oxygen from the lungs to cells
- Cooperativity
- The change in hemoglobin's ability to bind oxygen (oxygen affinity) as oxygen binds
NewsLab news
The Biomolecular Chemistry Lab (Nagatomo Lab) was launched
An Assistant Professor received the Excellent Research Award at the 49th Meeting of the Society for Chemistry and Micro-Nano Systems
A master's student received a Poster Award at the 84th Symposium on Analytical Chemistry
ResearchResearch themes
The lab analyzes the physical and chemical processes that occur at the interfaces and inside of micrometer-sized microparticles and tiny droplets, one single microparticle at a time, with the aim of controlling reactions. It is also working to clarify the mechanism of the cooperativity that hemoglobin shows.
*Illustrative imageMass transport inside the pores of microparticles
The lab places a single porous microparticle in a solution and studies, through spectroscopic measurements and from a reaction kinetics perspective, how a solute moves by adsorbing and desorbing inside the pores. It examines diffusion and migration inside the pores and mass transport at the pore entrances.
*Illustrative imageThe mechanism of hemoglobin cooperativity
In hemoglobin, the ease of binding oxygen changes once oxygen has bound; this is cooperativity. Cases that the widely known explanation based on quaternary structure changes cannot account for have been reported, and the lab investigates how the α and β chains are involved in cooperativity.
MembersFaculty
The Biomolecular Chemistry Lab's members are faculty, master's students, and undergraduate students.As of 2026
- Associate ProfessorShigenori Nagatomo
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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: “Laboratory Optical Microscope” Aliva Sahoo / CC BY-SA 4.0 (cropped)
- Mass transport inside the pores of microparticles: “Laboratory 2 Analytical Chemistry Dept Gdansk University of Technology” LukaszKatlewa / CC BY-SA 4.0 (cropped)
- The mechanism of hemoglobin cooperativity: “Red Blood Cell” Arek Socha / CC0 (cropped)
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