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Biophysical Chemistry Lab
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The lab uses NMR to observe the dynamics of biomolecules in detail and applies the findings to drug discovery.
AboutAbout the lab
Understanding life and drugs through molecular motion
The Biophysical Chemistry Lab studies how the molecules that sustain life move and function.
Using physical chemistry methods centered on nuclear magnetic resonance (NMR), the lab observes the dynamic behavior of molecules and seeks to clarify how those molecules contribute to the workings of the body.
The lab pursues "dynamic structure-based drug discovery," which actively applies the motions of proteins and RNA to drug discovery.
The lab also develops new NMR methods, such as measurements of high-molecular-weight proteins and analyses inside living cells.
Key terms
- Nuclear magnetic resonance (NMR)
- A method that investigates the shape and motion of molecules at the atomic level, using the signals emitted by atomic nuclei in a strong magnetic field
- GPCR
- A receptor in the cell membrane that transmits external stimuli into the cell. It is the target of many drugs
- Ligand
- A molecule that binds to a specific site on a protein or other molecule. It can be a drug candidate
NewsLab news
Developed an NMR technique that captures the dynamics of human membrane proteins with high sensitivity (Journal of the American Chemical Society)
A paper showing that the conformational equilibrium of RNA affects how inhibitors act was published in ACS Chem Biol
Elucidated part of the mechanism by which the RNA helicase DDX3X forms stress granules
Project Assistant Professor Yuki Toyama received the Young Scientists' Prize of the Commendation for Science and Technology by the Minister of Education, Culture, Sports, Science and Technology
A master's student received the Outstanding Presentation Award at the 146th Annual Meeting of the Pharmaceutical Society of Japan
ResearchResearch themes
Biomolecules such as proteins exert their functions by dynamically changing their structures. Taking advantage of NMR, which can quantify motion at the atomic level, the Biophysical Chemistry Lab investigates the relationship between molecular structure and function, and pursues "dynamic structure-based drug discovery" that applies molecular motion to drug development.
*Illustrative imageProteins that bind many drugs
Multidrug resistance is a major obstacle in the treatment of pathogenic bacteria and cancer. The lab uses NMR to study how multidrug-binding proteins, which bind strongly to a wide variety of drugs, recognize diverse molecules by dynamically changing their structures.
*Illustrative imageHow GPCRs are activated
GPCRs are the targets of many marketed drugs. The lab uses NMR to analyze how the equilibrium between active and inactive structures determines the efficacy of ligands, and applies the findings to drug discovery targeting GPCRs.
*Illustrative imageBuilding models of signal transduction
The lab integrates the conformational equilibria of receptors revealed by NMR with mathematical models built from cell-level studies, and develops models that explain the speed of signal transduction and its temperature sensitivity.
*Illustrative imageFinding hidden drug-binding sites
Cryptic sites are binding sites that appear to emerge only when a ligand binds. The lab uses NMR to find them in the ligand-free state, aiming to make drug development against difficult targets more efficient.
MembersFaculty
The members of the Biophysical Chemistry Lab consist of faculty, secretaries, technical staff, and doctoral, master's, and undergraduate students.As of 2026
- ProfessorKoh TakeuchiPublications ↗
- LecturerYutaka KofukuPublications ↗
- Assistant ProfessorYuki ToyamaPublications ↗
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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: “NMR Spectrometer” Mgianino / CC BY 3.0 (cropped)
- Proteins that bind many drugs: “Staphylococcus aureus VISA 2” Content Providers(s): CDC/ Matthew J. Arduino, DRPH Photo Credit: Janice Haney Carr / Public domain (cropped)
- How GPCRs are activated: “XBio illustration – G Protein Coupled Receptor (GPCR)” explorebiology / CC BY 4.0 (cropped)
- Building models of signal transduction: “Signal transduction pathways zh” File:Signal transduction pathways.png: Boghog2 at English Wikipedia derivative work: GnolizX / Public domain (cropped)
- Finding hidden drug-binding sites: “The green structures represent the cartoon representation of the protein's alpha-helices, while the grey surface shows the accessible molecular surface of the binding pocket” A / CC BY-SA 4.0 (cropped)
- Related lab (遺伝学教室): “Drosophila melanogaster under microscope” Talita Oliveira / CC BY-SA 4.0 (cropped)
- Related lab (生体分析化学教室): “Nikon-Inverted fluorescence microscope” ArthurLau1997 / CC BY 4.0 (cropped)
- Related lab (衛生化学教室): “Applied Biosystems 4000 QTrap Mass Spectrometer (detail) (11)” Hey Paul from Sacramento, CA, USA / CC BY 2.0 (cropped)
- Related lab (基礎有機化学教室): “Benzene IBO” Alicesu / CC BY-SA 4.0 (cropped)
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