Materials
Name | Company | Catalog Number | Comments |
Avance DMX 600 MHz Spectrometer | Bruker | ||
NMR sample tubes | Wilmad | 535-PP | |
Glove box | MBraun | LM05-019 | |
Lyophilizer | VirTis | benchtopK | |
Peptide | BioChemia | Custom made | >95% purity |
Copper (1) chloride | Aldrich | 224332 | |
Hydrochloric acid | BioLab | 231-595-7 | |
Sodium hydroxide | Gadot | 1310-73-2 | |
d6-Dimethylsulfoxide | Aldrich | 236926 | |
Deuterium oxide | Aldrich | 151882 |
References
- Robinson, J. A. Protein epitope mimetics as anti-infectives. Curr. Opin. Chem. Biol. 15, 379-386 (2011).
- Huffman, D. L., Function O'Halloran, T. V. structure, and mechanism of intracellular copper trafficking proteins. Annu. Rev. Biochem. 70, 677-701 (2001).
- Tapiero, H., Townsend, D. M., Tew, K. D. Trace elements in human physiology and pathology. Copper. Biomed., & Pharmacotherapy. 57, 386-398 (2003).
- Boal, A. K., Rosenzweig, A. C. Structural Biology of Copper Trafficking. Chem. Rev. 109, 4760-4779 (2009).
- Rubino, J. T., Franz, K. J. Coordination chemistry of copper proteins: How nature handles a toxic cargo for essential function. J. Inorg. Biochem. 107, 129-143 (2012).
- Wernimont, A. K., Huffman, D. L., Lamb, A. L., O'Halloran, T. V., Rosenzweig, A. C. Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Nat. Struct. Biol. 7, 766-771 (2000).
- Singleton, C., Hearnshaw, S., Zhou, L., Le Brun, N. E., Hemmings, A. M. Mechanistic insights into Cu(I) cluster transfer between the chaperone CopZ and its cognate Cu(I)-transporting P-type ATPase, CopA. Biochem. J. 424, 347-356 (2009).
- Hearnshaw, S., et al. A Tetranuclear Cu(I) Cluster in the Metallochaperone Protein CopZ. Biochem. 48, 9324-9326 (2009).
- Shoshan, M. S., Tshuva, E. Y. The MXCXXC class of metallochaperone proteins: model studies. Chem. Soc. Rev. 40, 5282-5292 (2011).
- Shoshan, M. S., et al. NMR characterization of a Cu(I)-bound peptide model of copper metallochaperones: Insights on the role of methionine. Chem. Comm. 47, 6407-6409 (2011).
- Schmitt, W., Zanotti, G., Wieland, T., Kessler, H. Conformation of different S-deoxo-Xaa(3)-amaninamide analogues in DMSO solution as determined by NMR spectroscopy. Strong CD effects induced by beta I, beta II conformational change. J. Am. Chem. Soc. 118 (3), 4380-4387 (1996).
- Behrens, S., Matha, B., Bitan, G., Gilon, C., Kessler, H. Structure-activity relationship of the ring portion in backbone-cyclic C-terminal hexapeptide analogs of substance P - NMR and molecular dynamics. Int. J. Peptide and Protein Res. 48, 569-579 (1996).
- Overview TopSpin NMR - Software for NMR Data Analysis and NMR Spectra Data Procession | Bruker Corporation [Internet]. , Bruker Corporation. Available from: http://www.bruker.com/products/mr/nmr/nmr-software/software/topspin (2013).
- Aue, W. P., Bartholdi, E., Ernst, R. R. 2-Dimensionsl spectroscopy- application to nuclear magnetic resonance. J. Chem. Phys. 64, 2229-2246 (1976).
- Bax, A., Davis, D. G. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 65, 355-360 (1985).
- Kumar, A., Ernst, R. R., Wüthrich, K. A two-dimensional nuclear overhauser enhancement (2D NO) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Comm. 95, 1-6 (1980).
- Bax, A., Davis, D. G. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 63, 207-213 (1985).
- Williamson, M. P. Chapter 3 Applications of the NOE in Molecular Biology. Annu. Reports on NMR Spectroscopy. 65, 77-109 (2009).
- Piotto, M., Saudek, V., Sklenar, V. Gradient-tailored excitation for single-quantum NMR-spectroscopy of aqueous solutions. J. Biomol. NMR. 2, 661-665 (1992).
- Sparky - NMR Assignment Program. , Available from: http://www.cgl.ucsf.edu/home/sparky (2008).
- Wüthrich, K. NMR of proteins and nucleic acids. , J. Wiley & Sons Inc. (1986).
- Nilges, M., Kuszewski, J., Brünger, A. T. Comp. aspects study biol. macromol. by NMR. , Plenum Press. (1991).
- Koradi, R., Billeter, M., Wüthrich, K. MOLMOL: A program for display and analysis of macromolecular structures. J. Molecular Graphics. 14, 51 (1996).
- Pettersen, E. F., et al. UCSF chimera - A visualization system for exploratory research and analysis. J. Computational Chem. 25, 1605-1612 (2004).
- Pearlmen, D. A., et al. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules. Comp. Phys. 91, 1-41 (1995).
- Honig, B., Sharp, K., Yang, A. S. Macroscopic models of aqueous solutions- biological and chemical applications. J. Phys. Chem. 97, 1101-1109 (1993).