BDR researchers coming from diverse research fields are working together to achieve higher goals.

Seminars & Symposia

Seminars & Symposia

BDR hosts annual symposium and regular seminars inviting international scientists in life science.

Careers & Study

Careers & Study

BDR embraces people from diverse backgrounds, and strives to create an open and supportive setting for research.



BDR communicates the appeal and significance of our research to society through the use of various media and activities.



From research, events, people and everything in between, find out what’s going on at RIKEN BDR.

About Us

About Us

Exploring the scientific foundations of life through interdisciplinary approaches to address society’s problems.

Photo of Team leder, Yoshitaka Ishii

Team Leader
Yoshitaka Ishii Ph.D.

Laboratory for Advanced NMR Application and Development

Location Yokohama / West NMR Bldg. N108


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Based at the internationally renowned NMR research center at the RIKEN Yokohama Campus, we develop world-leading high-field NMR methodologies and conduct advanced application research. In particular, we will work on development of NMR methods to elucidate the structures and functions of biomolecules such as amyloid proteins, RNA, and nano-biomaterials, which are difficult to analyze using conventional structural biology methods. We also develop advanced NMR methods suited for ultra-high-field NMR magnets that are under development at RIKEN as part of a JST-MIRAI project. It is also within our scope to explore novel NMR applications and NMR analysis integrated with electron microscopy and other methods.

Research Theme

  • Structural Biochemistry
  • Advanced nano-materials/ Polymer
  • Molecular mechanisms of Alzheimer's and other diseases

Selected Publications

Kashihara K, Oouchi M, Kodama Y, et al.
High-Field Nuclear Magnetic Resonance Studies Reveal New Structural Landscape of Sulfur-Vulcanized Natural Rubber.
Biomacromolecules 23(11), 4481-4492 (2022) doi: 10.1021/acs.biomac.2c00141

Matsunaga T, Okabe R, Ishii Y.
Efficient solvent suppression with adiabatic inversion for 1H-detected solid-state NMR.
Journal of Biomolecular NMR (2021) doi: 10.1007/s10858-021-00384-8

Wickramasinghe A, Xiao Y, Kobayashi N, et al.
Sensitivity-Enhanced Solid-State NMR Detection of Structural Differences and Unique Polymorphs in Pico- to Nanomolar Amounts of Brain-Derived and Synthetic 42-Residue Amyloid-β Fibrils.
Journal of the American Chemical Society 143(30), 11462-11472 (2021) doi: 10.1021/jacs.1c03346

Matsunaga T, Matsuda I, Yamazaki T, Ishii Y.
Decoherence optimized tilted-angle cross polarization: A novel concept for sensitivity-enhanced solid-state NMR using ultra-fast magic angle spinning.
Journal of Magnetic Resonance 322, 106857 (2021) doi: 10.1016/j.jmr.2020.106857

Koga R, Yamamoto M, Kosugi T, et al.
Robust folding of a de novo designed ideal protein even with most of the core mutated to valine.
Proceedings of the National Academy of Sciences of the United States of America 117(49), 31149-31156 (2020) doi: 10.1073/pnas.2002120117

Ohyama T, Takahashi H, Sharma H, et al.
An NMR-based approach reveals the core structure of the functional domain of SINEUP lncRNAs.
Nucleic Acids Research 48(16), 9346-9360 (2020) doi: 10.1093/nar/gkaa598

Xiao Y, Matsuda I, Inoue M, et al.
NMR-based site-resolved profiling of β-amyloid misfolding reveals structural transitions from pathologically relevant spherical oligomer to fibril.
the Journal of Biological Chemistry 295(2), 458-467 (2020) doi: 10.1074/jbc.RA119.008522

Oouchi M, Ukawa J, Ishii Y, Maeda H.
Structural Analysis of the Terminal Groups in Commercial Hevea Natural Rubber by 2D-NMR with DOSY Filters and Multiple-WET Methods Using Ultrahigh-Field NMR.
Biomacromolecules 20(3), 1394-1400 (2019) doi: 10.1021/acs.biomac.8b01771

Shi X, Prasanna C, Nagashima T, et al.
Structure and Dynamics in the Nucleosome Revealed by Solid-State NMR.
Angewandte Chemie 57(31), 9734-9738 (2018) doi: 10.1002/anie.201804707

Yoo BK, Xiao Y, McElheny D, Ishii Y.
E22G Pathogenic Mutation of β-Amyloid (Aβ) Enhances Misfolding of Aβ40 by Unexpected Prion-like Cross Talk between Aβ42 and Aβ40.
Journal of the American Chemical Society 140(8), 2781-2784 (2018) doi: 10.1021/jacs.7b13660

Xiao Y, Ma B, McElheny D, et al.
Aβ(1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease.
Nature Structural & Molecular Biology 22(6), 499-505 (2015) doi: 10.1038/nsmb.2991

Parthasarathy S, Inoue M, Xiao Y, et al.
Structural Insight into an Alzheimer's Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR.
Journal of the American Chemical Society 137(20), 6480-3 (2015) doi: 10.1021/jacs.5b03373

Wickramasinghe NP, Parthasarathy S, Jones CR, et al.
Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries.
Nature Methods 6(3), 215-8 (2009) doi: 10.1038/nmeth.1300


Yoshitaka Ishii

Team Leader

Naohiro Kobayashi

Senior Scientist

Masato Takahashi

Senior Scientist

Takako Ohyama

Research Scientist

Ayesha Wijalath Pelige

Research Scientist

Mohammad JafarTehrani

Research Associate

Kyoko Seimiya

Technical Staff I