Laboratory for Molecular Biophysics
Institute for Protein Research

Associate Professor

Yoh MATSUKI

yohConcurrent Associate Professor

Yohei MIYANOIRI

y-miyanoiri

URL: http://www.protein.osaka-u.ac.jp/biophys/
In our bodies, various energy andinformation transformations arecarried out through biologicalmembranes. The supramolecularsystems that carry out thesefunctions play an important role in
the networking of biological activities.
Currently, the structures ofmolecules with these functions arebeing revealed one after another.
Our research aims to elucidate thefunction of proteins responsible forFurthermore, we analyze how the protein
information and energy conversion
interacts with other proteins or ligands toon the basis of their threeregulate its function at high structuraldimensional structures, mainly using resolution. We are also finding thenuclear magnetic resonance (NMR). correlation of the protein activity with thedynamics on relatively slow time scales,
Structure and function analysis ofmicroseconds and milliseconds. Since theproteins by solid-state NMR
methodologies required for these analyses
are still in the early stage, we are also
Solid-state NMR reveals structure anddeveloping such methodologies in NMR
function of biologically important molecularexperiments and sample preparation suchcomplexes that not amenable to X-ray
as isotope labeling.
crystallography and electron microscopy. We
are working on the structure and function
Research Topics
analysis of molecular complex systems thatare important for the signal transduction in
1. Atomic resolution analysis of protein
living organisms. Specifically, these include
function and structure in cells
proteins strongly bound to lipid bilayers andlarge molecular complexes in an amorphous
2. Structural and functional analysis ofstate, such as rhodopsin, a membrane protein
amyloid proteinsthat transmits optical information, G proteinsin complex with their receptors, and amyloid
3. Structural analysis of membraneproteins. In addition, we are addressing
proteins for signal transduction
structural and interaction analysis of proteinssite-selectively in cells. As in biology, NMR
4. Development of NMR structuralexperimental and analytical methods haveanalysis based on selective isotope
also made great progress. We are developing
labeling
experimental and data analysis methods for
extracting more detailed information based on 5. Analysis of protein structure andsolid-state magnetic interactions.
conformational change usingparamagnetic probe molecules
Structure and function analysis of
6. Development of NMR structuralproteins by solution NMR
analysis using bioinformatics
NMR is a very useful tool for analyzing theconformation and dynamics of proteins at theatomic level in the physiological solution states.
In this laboratory, the 3D structures of proteins
are mainly analyzed by NMR.

7. Development of ultra-highly sensitive
NMR using terahertz waves and its
application to biological systems

Fig. 1 Two-dimensional NMR spectra
showing protein-protein interactions and theinteraction between protein ubiquitin andYUH revealed by NMR.

Figure 2 Ultra-highly sensitive DNP-NMRspectrometer. A superconducting magnet (left) and aterahertz-wave light source, a gyrotron (right), areused to observe NMR at cryogenic temperatures.

Institute for Protein Research, Osaka University
3-2 Yamadaoka, Suita, Osaka 565-0871, Japan
TEL: +81-6-6879-8598
FAX : +81-6-6879-8599
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