Molecular Structures Core (MSC)
The Molecular Structures Core (MSC) enables researchers to determine the structures and dynamics, or motions, of large biomolecules such as proteins and DNA to understand how they interact with each other and with small molecules such as drugs.
RRID:SCR_022888
Visit Us!
Location:
Biological Sciences West, Room 201
Staff Hours:
By appointment only
24/7 access for Trained Users
Services
The Bruker Avance NEO 800 MHz and 600 MHz NMR systems are optimized for biomolecular applications. Both are equipped with TCI cryoprobes for unparalleled signal-to-noise, allowing acquisition of protein spectra at as low as 10 μM concentration. The systems are capable of direct detection of 1H, 2H, 13C, 15N, and 19F, and all channels other than 2H have the sensitivity advantage of cryo-cooled electronics.
Education/Outreach
Molecular Structures Core is committed to serving scientists and students at the University of Arizona. We support NMR teaching labs, such as CHEM447, NMR Summer Workshops, and regularly provide educational demonstrations to students. We also provide services and consultation to researchers within and outside of the University of Arizona, and have a wide range of experiments and expertise to match our diverse user base.
Facility Publications
Use the MSC Facility RRID!
University of Arizona - UA CBC Molecular Structures Core (MSC), RRID:SCR_022888
Koss, K. M., Sereda, T. J., Kumirov, V. K., & Wertheim, J. A. (2023). A class of peptides designed to replicate and enhance the Receptor for Hyaluronic Acid Mediated Motility binding domain. _Acta Biomaterialia_.
Ambrose, A. J., Sivinski, J., Zerio, C. J., Zhu, X., Godek, J., Kumirov, V. K., ... & Chapman, E. (2022). Discovery and Development of a Selective Inhibitor of the ER Resident Chaperone Grp78. _Journal of Medicinal Chemistry_.
Zhang, R., Kumar, G. S., Hansen, U., Zoccheddu, M., Sacchetti, C., Holmes, Z. J., ... & Bottini, N. (2022). Oxidative stress promotes fibrosis in systemic sclerosis through stabilization of a kinase-phosphatase complex. _JCI insight_, _7_(8).
Torgeson, K. R., Clarkson, M. W., Granata, D., Lindorff-Larsen, K., Page, R., & Peti, W. (2022). Conserved conformational dynamics determine enzyme activity. _Science advances_, _8_(31), eabo5546.
Vos, M. R., Piraino, B., LaBreck, C. J., Rahmani, N., Trebino, C. E., Schoenle, M., ... & Page, R. (2022). Degradation of the E. coli antitoxin MqsA by the proteolytic complex ClpXP is regulated by zinc occupancy and oxidation. _Journal of Biological Chemistry_, _298_(2).
Goodman, H., Tanguturi, P., Szabo, L., Sprober, S., Liu, C., Al-Obeidi, F., ... & Polt, R. (2022). Structure-based design of glycosylated oxytocin analogues with improved selectivity and antinociceptive activity.
Singh, J. P., Li, Y., Chen, Y. Y., Hsu, S. T. D., Page, R., Peti, W., & Meng, T. C. (2022). The catalytic activity of TCPTP is auto-regulated by its intrinsically disordered tail and activated by Integrin alpha-1. _Nature Communications_, _13_(1), 1-12.
Schoenle, M. V., Li, Y., Yuan, M., Clarkson, M. W., Wilson, I. A., Peti, W., & Page, R. (2021). NMR Based SARS-CoV-2 Antibody Screening. _Journal of the American Chemical Society_, _143_(21), 7930-7934.
Fowle, H., Zhao, Z., Xu, Q., Wasserman, J. S., Wang, X., Adeyemi, M., ... & Graña, X. (2021). PP2A/B55α substrate recruitment as defined by the retinoblastoma-related protein p107. _Elife_, _10_, e63181.
Bearss, J. J., Padi, S. K., Singh, N., Cardo‐Vila, M., Song, J. H., Mouneimne, G., ... & Okumura, K. (2021). EDC3 phosphorylation regulates growth and invasion through controlling P‐body formation and dynamics. _EMBO reports_, _22_(4), e50835.
Fowle, H., Zhao, Z., Xu, Q., Wasserman, J. S., Wang, X., Adeyemi, M., ... & Graña, X. (2021). Pp2a/b55a substrate recruitment as defined by the retinoblastoma-related protein p107.
Li, Y., Sheftic, S. R., Grigoriu, S., Schwieters, C. D., Page, R., & Peti, W. (2020). The structure of the RCAN1: CN complex explains the inhibition of and substrate recruitment by calcineurin. _Science advances_, _6_(27), eaba3681.
Torgeson, K. R., Clarkson, M. W., Kumar, G. S., Page, R., & Peti, W. (2020). Cooperative dynamics across distinct structural elements regulate PTP1B activity. _Journal of Biological Chemistry_, _295_(40), 13829-13837.
Wang, X., Garvanska, D. H., Nasa, I., Ueki, Y., Zhang, G., Kettenbach, A. N., ... & Page, R. (2020). A dynamic charge-charge interaction modulates PP2A: B56 substrate recruitment. _Elife_, _9_, e55966.
Kumar, G. S., Page, R., & Peti, W. (2020). The mode of action of the Protein tyrosine phosphatase 1B inhibitor Ertiprotafib. _Plos one_, _15_(10), e0240044.
Kump, K. J., Miao, L., Mady, A. S., Ansari, N. H., Shrestha, U. K., Yang, Y., ... & Nikolovska-Coleska, Z. (2020). Discovery and characterization of 2, 5-substituted benzoic acid dual inhibitors of the anti-apoptotic Mcl-1 and Bfl-1 proteins. _Journal of medicinal chemistry_, _63_(5), 2489-2510.
Sok, P., Gógl, G., Kumar, G. S., Alexa, A., Singh, N., Kirsch, K., ... & Reményi, A. (2020). MAP kinase-mediated activation of RSK1 and MK2 substrate kinases. _Structure_, _28_(10), 1101-1113.
Kirsch, K., Zeke, A., Tőke, O., Sok, P., Sethi, A., Sebő, A., ... & Reményi, A. (2020). Co-regulation of the transcription controlling ATF2 phosphoswitch by JNK and p38. _Nature communications_, _11_(1), 1-15.
Lixa, C., Clarkson, M. W., Iqbal, A., Moon, T. M., Almeida, F. C., Peti, W., & Pinheiro, A. S. (2019). Retinoic acid binding leads to CRABP2 rigidification and dimerization. _Biochemistry_, _58_(41), 4183-4194.
Hendus-Altenburger, R., Wang, X., Sjøgaard-Frich, L. M., Pedraz-Cuesta, E., Sheftic, S. R., Bendsøe, A. H., ... & Peti, W. (2019). Molecular basis for the binding and selective dephosphorylation of Na+/H+ exchanger 1 by calcineurin. _Nature communications_, _10_(1), 1-13.
François-Moutal, L., Felemban, R., Scott, D. D., Sayegh, M. R., Miranda, V. G., Perez-Miller, S., ... & Khanna, M. (2019). Small molecule targeting TDP-43's RNA recognition motifs reduces locomotor defects in a Drosophila model of amyotrophic lateral sclerosis (ALS). _ACS chemical biology_, _14_(9), 2006-2013.
Scott, D. D., Francois-Moutal, L., Kumirov, V. K., & Khanna, M. (2019). 1H, 15N and 13C backbone assignment of apo TDP-43 RNA recognition motifs. _Biomolecular NMR assignments_, _13_(1), 163-167.
Bertran, M. T., Mouilleron, S., Zhou, Y., Bajaj, R., Uliana, F., Kumar, G. S., ... & Tapon, N. (2019). ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail. _Nature communications_, _10_(1), 1-19.
Kumar, G. S., Choy, M. S., Koveal, D. M., Lorinsky, M. K., Lyons, S. P., Kettenbach, A. N., Page, R., & Peti, W. (2018). Identification of the substrate recruitment mechanism of the muscle glycogen protein phosphatase 1 holoenzyme. _Science Advances_, _4_(11), eaau6044.
François-Moutal, L., Scott, D. D., Perez-Miller, S., Gokhale, V., Khanna, M., & Khanna, R. (2018). Chemical shift perturbation mapping of the Ubc9-CRMP2 interface identifies a pocket in CRMP2 amenable for allosteric modulation of Nav1. 7 channels. _Channels_, _12_(1), 219-227.