We offer investigators the latest instrumentation and expertise.
NMR Facility for Biological Research
in the Center for Structural Biology
NMR Facility for Biological Research
About
The NMR Facility for Biological Research operates six NMR spectrometers with proton resonance frequencies from 850 to 500 MHz. Four of the highest field spectrometers (850, 800, 700, 600) are equipped with helium cooled cryoprobes optimized for high-resolution experiments on biological samples in solutions. These high field instruments are dedicated to research projects conducted by laboratories within Center for Structural Biology.
The second 600 MHz spectrometer is set up as reconfigurable development system with multiple probes allowing for high-resolution liquid state as well as biosolids Magic Angle Spinning (MAS) experiments and is sometimes used to perform experiments with special purpose probes.
The Facility operates a fully automated 500 MHz spectrometer designated as an “open access” instrument to all of the FNLCR community. This spectrometer is equipped with broadband X-H/F type nitrogen cooled cryoprobe which is optimized for work on small molecule samples and serves as an analytical tool for a large number of users – particularly from the Chemical Biology Laboratory.
Publications
NMR Selected Recent Publications:
A sampling of recent publications from the NMR Facility is presented below.
2025
Lu, X., Sabbasani, V. R., Hassan, B., Swenson, R. E. & Walters, K. J.: “Optimization of the PROTAC linker region of the proteasome substrate receptor hRpn13 rationalized structural modeling with molecular dynamics.” (2025) Journal of Biological Chemistry Apr 18:108520. doi: 10.1016/j.jbc.2025.108520. Epub ahead of print. PMID: 40254254.
Bregnard, T.A., Fairchild, D., Chen, X., Erlandsen, H., Tarasov, S.G., Walters, K.J., Korzhnev, D.M., and Bezsonova, I. (2025). Differences in structure, dynamics, and zinc coordination between isoforms of human ubiquitin ligase UBE3A. J Biol Chem 301, 108149. 10.1016/j.jbc.2024.108149.
Hassan, B., Chandravanshi, M., Ng, M.Y., Negi, H., Wilson, B.A.P., and Walters, K.J. (2025). An adaptivepeptide-binding site in ubiquitin receptor hRpn13 revealed by structural studies. Nature Communications 16, 5669. 10.1038/s41467-025-60843-w.
Hedger AK, Myint W, Lee JM, Suchenski Loustaunau D, Balachandran V, Shaqra AM, Kurt Yilmaz N, Watts JK, Matsuo H, Schiffer CA. Next generation APOBEC3 inhibitors: optimally designed for potency and nuclease stability. Nucleic Acids Res. 2025 Mar 20;53(6):gkaf234. doi: 10.1093/nar/gkaf234. PMID: 40156866; PMCID: PMC11954526.
2024
Folimonova, V., Chen, X., Negi, H., Schwieters, C. D., Li, J., Byrd, R. A., Taylor, N., Youkharibache, P., Walters K. J.: “CD28 hinge used in chimeric antigen receptor (CAR) T-cells exhibits local structure and conformational exchange amidst global disorder” (2024) Nat. Commun. Biol. 7, 1072. https://doi.org/10.1038/s42003-024-06770-w
Osei-Amponsa, V., Chandravanshi, M., Lu, X., Magidson, V., Das, S., Andresson, T., Dyba, M., Sabbasani, V. R., Swenson, R. E., Fromont, C., Shrestha, B., Zhao, Y., Clapp, M. E., Chari, R., Walters, K. J.: “hRpn13 shapes the proteome and transcriptome through epigenetic factors HDAC8, PADI4 and transcription factor NF-kB p50” Molecular Cell (2024) 84, 522-537. doi: 10.1016/j.molcel.2023.11.035. PMID: 38151017.
Lu, X., Chandravanshi, M., Sabbasani, V.R., Gaikwad, S., Hughitt, V. K., Gyabaah-Kessie, N., Scroggins, B. T., Das, S., Myint, W., Clapp, M. E., Schwieters, C. D., Dyba, M., Bolhuis, D. L., Janusz W. Koscielniak, Andresson, T., Brown, N. G., Emanuele, M. J., Matsuo, H., Chari, R., Citrin, D. E., Mock, B. A., Swenson, R. E., Walters, K. J.: “A structure-based designed small molecule depletes hRpn13Pru and a select group of KEN box proteins” Nature Communications (2024) 15, 2485. https://doi.org/10.1038/s41467-024-46644-7
2023
Buel, G. R., Chen, X., Myint, W., Kayode, O., Folimonova, V., Cruz, A., Skorupka, K. A., Matsuo, H., Walters, K. J. E6AP AZUL interaction with UBQLN1/2 in cells, condensates, and an AlphaFold-NMR integrated structure. Structure 31(4), 395-410 (2023). doi: https://doi.org/10.1016/j.str.2023.01.012
Buel, G. R., Chen, X., Kayode, O., Cruz, A., and Walters, K. J. 1H, 15N, 13C backbone and Cb resonance assignments for UBQLN1 UBA and UBAA domains. Biomol. NMR assign. (2023) https://doi.org/10.1007/s12104-023-10127-5.
Contact
Contact Info
Center for Cancer Research National Cancer Institute
- Building 538, Room 187
- Frederick, MD 21702
- 301-846-5213
