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Biophysical Chemistry and Structural Life Chemistry Lab
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The lab uses NMR as its core method to investigate the three-dimensional structures of biomolecules and how they bind to one another.
AboutAbout the lab
Unraveling how biomolecules bind, with NMR
The Biophysical Chemistry and Structural Life Chemistry Lab studies the highly specific intermolecular interactions that underlie the functions of biological macromolecules.
The lab mainly uses solution NMR, combining its own sample preparation and NMR structure analysis techniques with physical chemistry methods such as particle measurement and calorimetry, as well as computational methods such as AI.
It investigates biological functions from two sides: analysis of the three-dimensional structures of biological macromolecules, and the equilibrium and kinetics of dissociation and association.
On the lab's website, it is introduced under the name "Kojima Lab."
Key terms
- NMR
- Nuclear magnetic resonance. An analytical method that can determine the three-dimensional structures of molecules under physiological conditions, and the core of this lab's research
- Biological macromolecules
- Large molecules that function inside living organisms, such as proteins and nucleic acids
- Isothermal titration calorimeter
- A device that measures the heat released or absorbed when molecules bind to each other
NewsLab news
Paper on the structural mechanism of VAPB protein condensate formation published in Scientific Reports
Paper from a joint study with Kyushu University published in Magnetic Resonance in Chemistry
Paper with a doctoral student as first author published in Methods and Protocols
Particle size measurement achieved with a general-purpose plate reader; press release issued
Paper on estimating the size of LLPS droplets with a plate reader published in Scientific Reports
ResearchResearch themes
With NMR at its core, the lab works to solve the mysteries of biological macromolecules and life processes, and takes on the challenge of controlling biological phenomena with chemical compounds. The lab's website describes NMR as the only method that enables three-dimensional structure analysis under physiological conditions.
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MembersFaculty
The members of the Biophysical Chemistry and Structural Life Chemistry Lab consist of faculty members, researchers, master's and undergraduate students, and ROUTE (second-year undergraduate) students.As of 2026
- ProfessorChojiro Kojima
- Assistant ProfessorShuhei Sakurabayashi
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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: “ANKRD35 protein structure” 1. Yang Zhang. I-TASSER: Fully automated protein structure prediction in CASP8. Proteins, 77 (Suppl 9): 100-113, 2009. 2. Ambrish Roy, Jianyi Yang, Yang Zhang. COFACTOR: an accurate comparative algorithm for structure-based protein function annotation. Nucleic Acids Research, 40: W471-W477, 2012. 3. Jianyi Yang, Yang Zhang. I-TASSER server: new development for protein structure and function predictions, Nucleic Acids Research, 43: W174-W181, 2015. / CC BY-SA 4.0 (cropped)
- Structural and Functional Analysis Centered on NMR: “NMR spectrometer” Daniel Alexandre / CC BY-SA 3.0 (cropped)
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- Related lab (Nittami Lab): “Secondary treatment reactors - Blue Plains WWTP - 2016b” Moreau1 / Public domain (cropped)
- Related lab (Biorelated Chemistry Lab): “Hydrogel ( )” National Institute of Standards and Technology / Public domain (cropped)
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