Frankenstein Bio Reagents
D31-LDAO
- Hiller, S., Garces, R. G., Malia, T. J., Orekhov, V. Y., Colombini, M., & Wagner, G. (2008). Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science, 321(5893), 1206-1210.
- Hiller, S., Ibraghimov, I., Wagner, G., & Orekhov, V. Y. (2009). Coupled decomposition of four-dimensional NOESY spectra. Journal of the American Chemical Society, 131(36), 12970-12978.
- Hiller, S., Malia, T. J., Garces, R. G., Orekhov, V. Y., & Wagner, G. (2010). Backbone and ILV side chain methyl group assignments of the integral human membrane protein VDAC-1. Biomolecular NMR assignments, 4, 29-32.
- Yu, T. Y., Raschle, T., Hiller, S., & Wagner, G. (2012). Solution NMR spectroscopic characterization of human VDAC-2 in detergent micelles and lipid bilayer nanodiscs. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1818(6), 1562-1569.
- Bayrhuber, M., Maslennikov, I., Kwiatkowski, W., Sobol, A., Wierschem, C., Eichmann, C., … & Riek, R. (2019). Nuclear magnetic resonance solution structure and functional behavior of the human proton channel. Biochemistry, 58(39), 4017-4027.
- Eddy, M. T., Yu, T. Y., Wagner, G., & Griffin, R. G. (2019). Structural characterization of the human membrane protein VDAC2 in lipid bilayers by MAS NMR. Journal of biomolecular NMR, 73(8), 451-460.
- Böhm, R., Amodeo, G. F., Murlidaran, S., Chavali, S., Wagner, G., Winterhalter, M., … & Hiller, S. (2020). The structural basis for low conductance in the membrane protein VDAC upon β-NADH binding and voltage gating. Structure, 28(2), 206-214.
- Günsel, U., Klöpfer, K., Häusler, E., Hitzenberger, M., Bölter, B., Sperl, L. E., … & Hagn, F. (2023). Structural basis of metabolite transport by the chloroplast outer envelope channel OEP21. Nature Structural & Molecular Biology, 30(6), 761-769.
D54-DMPC
- Hagn, F., Etzkorn, M., Raschle, T., & Wagner, G. (2013). Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins. Journal of the American Chemical Society, 135(5), 1919-1925.
- Hagn, F., & Wagner, G. (2015). Structure refinement and membrane positioning of selectively labeled OmpX in phospholipid nanodiscs. Journal of biomolecular NMR, 61, 249-260.
- Bibow, S., Polyhach, Y., Eichmann, C., Chi, C. N., Kowal, J., Albiez, S., … & Riek, R. (2017). Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein AI. Nature structural & molecular biology, 24(2), 187-193.
- Cuevas Arenas, R., Danielczak, B., Martel, A., Porcar, L., Breyton, C., Ebel, C., & Keller, S. (2017). Fast collisional lipid transfer among polymer-bounded nanodiscs. Scientific reports, 7(1), 45875.
- Hagn, F., Nasr, M. L., & Wagner, G. (2018). Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR. Nature protocols, 13(1), 79-98.
- Bibow, S. (2019). Opportunities and challenges of backbone, sidechain, and RDC experiments to study membrane protein dynamics in a detergent-free lipid environment using solution state NMR. Frontiers in molecular biosciences, 6, 103.
- Schuster, M., Deluigi, M., Pantić, M., Vacca, S., Baumann, C., Scott, D. J., … & Zerbe, O. (2020). Optimizing the α1B-adrenergic receptor for solution NMR studies. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1862(10), 183354.
- Piai, A., Fu, Q., Cai, Y., Ghantous, F., Xiao, T., Shaik, M. M., … & Chou, J. J. (2020). Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein. Nature communications, 11(1), 2317.
- Bibow, S., Böhm, R., Modaresi, S. M., & Hiller, S. (2020). Detergent titration as an efficient method for NMR resonance assignments of membrane proteins in lipid–bilayer nanodiscs. Analytical chemistry, 92(11), 7786-7793.
- Gaussmann, S., Gopalswamy, M., Eberhardt, M., Reuter, M., Zou, P., Schliebs, W., … & Sattler, M. (2021). Membrane interactions of the peroxisomal proteins PEX5 and PEX14. Frontiers in Cell and Developmental Biology, 9, 651449.
- Daniilidis, M., Brandl, M. J., & Hagn, F. (2022). The advanced properties of circularized MSP nanodiscs facilitate high-resolution NMR studies of membrane proteins. Journal of Molecular Biology, 434(24), 167861.
- Daniilidis, M., Brandl, M. J., & Hagn, F. (2022). The advanced properties of circularized MSP nanodiscs facilitate high-resolution NMR studies of membrane proteins. Journal of Molecular Biology, 434(24), 167861.
D54-DMPG
- Hagn, F., Etzkorn, M., Raschle, T., & Wagner, G. (2013). Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins. Journal of the American Chemical Society, 135(5), 1919-1925.
- Hagn, F., & Wagner, G. (2015). Structure refinement and membrane positioning of selectively labeled OmpX in phospholipid nanodiscs. Journal of biomolecular NMR, 61, 249-260.
- Hagn, F., Nasr, M. L., & Wagner, G. (2018). Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR. Nature protocols, 13(1), 79-98.
- Schuster, M., Deluigi, M., Pantić, M., Vacca, S., Baumann, C., Scott, D. J., … & Zerbe, O. (2020). Optimizing the α1B-adrenergic receptor for solution NMR studies. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1862(10), 183354.
- Gaussmann, S., Gopalswamy, M., Eberhardt, M., Reuter, M., Zou, P., Schliebs, W., … & Sattler, M. (2021). Membrane interactions of the peroxisomal proteins PEX5 and PEX14. Frontiers in Cell and Developmental Biology, 9, 651449.
- Daniilidis, M., Brandl, M. J., & Hagn, F. (2022). The advanced properties of circularized MSP nanodiscs facilitate high-resolution NMR studies of membrane proteins. Journal of Molecular Biology, 434(24), 167861.
D62-DOPC
- Motlaq, V. F., Adlmann, F. A., Hernández, V. A., Vorobiev, A., Wolff, M., & Bergström, L. M. (2022). Dissolution mechanism of supported phospholipid bilayer in the presence of amphiphilic drug investigated by neutron reflectometry and quartz crystal microbalance with dissipation monitoring. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1864(10), 183976.
- Scheidt, H. A., Kolocaj, K., Konrad, D. B., Frank, J. A., Trauner, D., Langosch, D., & Huster, D. (2020). Light-induced lipid mixing implies a causal role of lipid splay in membrane fusion. Biochimica et Biophysica Acta (BBA)-Biomembranes, 1862(11), 183438.
D22-D6PC
- Laguerre, A., Löhr, F., Henrich, E., Hoffmann, B., Abdul-Manan, N., Connolly, P. J., … & Dötsch, V. (2016). From nanodiscs to isotropic bicelles: a procedure for solution nuclear magnetic resonance studies of detergent-sensitive integral membrane proteins. Structure, 24(10), 1830-1841.
- Piai, A., Fu, Q., Cai, Y., Ghantous, F., Xiao, T., Shaik, M. M., … & Chou, J. J. (2020). Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein. Nature communications, 11(1), 2317.
D26-D7PC
- Mohamadi, M., Goricanec, D., Wagner, G., & Hagn, F. (2023). NMR sample optimization and backbone assignment of a stabilized neurotensin receptor. Journal of structural biology, 215(2), 107970.
- O’Brien, E. S., Lin, D. W., Fuglestad, B., Stetz, M. A., Gosse, T., Tommos, C., & Wand, A. J. (2018). Improving yields of deuterated, methyl labeled protein by growing in H 2 O. Journal of biomolecular NMR, 71, 263-273.
D78-DPhPC
- Barbet-Massin, E., Pell, A. J., Retel, J. S., Andreas, L. B., Jaudzems, K., Franks, W. T., … & Pintacuda, G. (2014). Rapid proton-detected NMR assignment for proteins with fast magic angle spinning. Journal of the American Chemical Society, 136(35), 12489-12497.
- Stampolaki, Μ., Hoffmann, A., Tekwani, K., Georgiou, K., Tzitzoglaki, C., Ma, C., … & Kolocouris, A. (2023). A Study of the Activity of Adamantyl Amines against Mutant Influenza A M2 Channels Identified a Polycyclic Cage Amine Triple Blocker, Explored by Molecular Dynamics Simulations and Solid‐State NMR. ChemMedChem, 18(16), e202300182.
- Andreas, L. B., Reese, M., Eddy, M. T., Gelev, V., Ni, Q. Z., Miller, E. A., … & Griffin, R. G. (2015). Structure and mechanism of the influenza A M218–60 dimer of dimers. Journal of the American Chemical Society, 137(47), 14877-14886.
D87-DPhPC
- Movellan, K. T., Wegstroth, M., Overkamp, K., Leonov, A., Becker, S., & Andreas, L. B. (2023). Real-time tracking of drug binding to influenza A M2 reveals a high energy barrier. Journal of Structural Biology: X, 8, 100090.
- Nimerovsky, E., Movellan, K. T., Zhang, X. C., Forster, M. C., Najbauer, E., Xue, K., … & Andreas, L. B. (2021). Proton detected solid-state NMR of membrane proteins at 28 Tesla (1.2 GHz) and 100 kHz magic-angle spinning. Biomolecules, 11(5), 752.
- Stampolaki, M., Varkey, A., Nimerovsky, E., Leonov, A., & Becker, S. (2024). Seeing double: the persistent dimer-of-dimers structure of drug resistant influenza A M2.
D25 -DDM
- Toyama, Y., & Shimada, I. (2019). Frequency selective coherence transfer NMR spectroscopy to study the structural dynamics of high molecular weight proteins. Journal of Magnetic Resonance, 304, 62-77.
- Bumbak, F., Pons, M., Inoue, A., Paniagua, J.C., Yan, F., Wu, H., Robson, S.A., Bathgate, R.A., Scott, D.J., Gooley, P.R. and Ziarek, J.J., 2023. Ligands selectively tune the local and global motions of neurotensin receptor 1 (NTS1). Cell reports, 42(1).
D27-LMPG
- Klammt, C., Maslennikov, I., Bayrhuber, M., Eichmann, C., Vajpai, N., Chiu, E. J. C., … & Choe, S. (2012). Facile backbone structure determination of human membrane proteins by NMR spectroscopy. Nature methods, 9(8), 834-839.
- Brady, J. P., Claridge, J. K., Smith, P. G., & Schnell, J. R. (2015). A conserved amphipathic helix is required for membrane tubule formation by Yop1p. Proceedings of the National Academy of Sciences, 112(7), E639-E648.
- Taylor, K. C., Kang, P. W., Hou, P., Yang, N. D., Kuenze, G., Smith, J. A., … & Sanders, C. R. (2020). Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state. Elife, 9, e53901.
D31-LPPG
- Brazin, K. N., Mallis, R. J., Li, C., Keskin, D. B., Arthanari, H., Gao, Y., … & Reinherz, E. L. (2014). Constitutively oxidized CXXC motifs within the CD3 heterodimeric ectodomains of the T cell receptor complex enforce the conformation of juxtaposed segments. Journal of Biological Chemistry, 289(27), 18880-18892.
- Chadwick, A. C., Jensen, D. R., Hanson, P. J., Lange, P. T., Proudfoot, S. C., Peterson, F. C., … & Sahoo, D. (2017). NMR structure of the C-terminal transmembrane domain of the HDL receptor, SR-BI, and a functionally relevant leucine zipper motif. Structure, 25(3), 446-457.
- Brazin, K. N., Mallis, R. J., Boeszoermenyi, A., Feng, Y., Yoshizawa, A., Reche, P. A., … & Reinherz, E. L. (2018). The T cell antigen receptor α transmembrane domain coordinates triggering through regulation of bilayer immersion and CD3 subunit associations. Immunity, 49(5), 829-841.
13C-Methyl amino acid precursors
- Gross, J. D. et al. A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes. J. Biomol. NMR 2003, 25, 235.
- Ito, T. et al. Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. Structure 2004, 12, 1693.
- Park, S. et al. Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 2005, 13, 995.
- Reibarkh, M. et al. Identification of individual protein-ligand NOEs in the limit of intermediate exchange. J. Biomol. NMR 2006, 36, 1.
- Hiller, S. et al. Backbone and ILV side chain methyl group assignments of the integral human membrane protein VDAC-1 J. Biomol. NMR. Nov. 22 2009.
- Linser, R., Gelev, V., Hagn, F., Arthanari, H., Hyberts, S. G., & Wagner, G. (2014). Selective methyl labeling of eukaryotic membrane proteins using cell-free expression. Journal of the American Chemical Society, 136(32), 11308-11310.
- De Paula, V. S., Dubey, A., Arthanari, H., & Sgourakis, N. G. (2020). A slow-exchange conformational switch regulates off-target cleavage by high-fidelity Cas9. bioRxiv, 2020-12.
- Nerli, S., De Paula, V. S., McShan, A. C., & Sgourakis, N. G. (2021). Backbone-independent NMR resonance assignments of methyl probes in large proteins. Nature communications, 12(1), 691.
13C-Methyl-Leucine
- Dubey, A., Stoyanov, N., Viennet, T., Chhabra, S., Elter, S., Borggräfe, J., … & Arthanari, H. (2021). Local deuteration enables NMR observation of methyl groups in proteins from eukaryotic and cell‐free expression systems. Angewandte Chemie International Edition, 60(25), 13783-13787.
- Mallis, R. J., Lee, J. J., Berg, A. V. D., Brazin, K. N., Viennet, T., Zmuda, J., … & Arthanari, H. (2024). Efficient and economic protein labeling for NMR in mammalian expression systems: Application to a preT‐cell and T‐cell receptor protein. Protein Science, 33(4), e4950.