The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability

Nature Protocols - Tập 2 Số 9 - Trang 2212-2221 - 2007
F. Niesen1, H. Berglund, Masoud Vedadi
1Structural Genomics Consortium, Botnar Research Centre, Oxford University, Oxford, UK. [email protected]

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Tài liệu tham khảo

Schellman, J.A. Temperature, stability, and the hydrophobic interaction. Biophys. J. 73, 2960–2964 (1997).

Privalov, P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33, 167–241 (1979).

Brandts, J.F. Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 29, 6927–6940 (1990).

Matulis, D., Kranz, J.K., Salemme, F.R. & Todd, M.J. Thermodynamic stability of carbonic anhydrase: measurements of binding affinity and stoichiometry using ThermoFluor. Biochemistry 44, 5258–5266 (2005).

Senisterra, G.A. et al. Screening for ligands using a generic and high-throughput light-scattering-based assay. J. Biomol. Screen. 11, 940–948 (2006).

Vedadi, M. et al. Chemical screening methods to identify ligands that promote protein stability, protein crystallization, and structure determination. Proc. Natl. Acad. Sci. USA 103, 15835–15840 (2006).

Holdgate, G.A. & Ward, W.H. Measurements of binding thermodynamics in drug discovery. Drug Discov. Today 10, 1543–1550 (2005).

Poklar, N., Lah, J., Salobir, M., Macek, P. & Vesnaver, G. pH and temperature-induced molten globule-like denatured states of equinatoxin II: a study by UV-melting, DSC, far- and near-UV CD spectroscopy, and ANS fluorescence. Biochemistry 36, 14345–14352 (1997).

Pantoliano, M.W. et al. High-density miniaturized thermal shift assays as a general strategy for drug discovery. J. Biomol. Screen. 6, 429–440 (2001).

Lo, M.-C. et al. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. 332, 153–159 (2004).

Ericsson, U.B., Hallberg, M.B., DeTitta, G.T., Dekker, N. & Nordlund, P. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 357, 289–298 (2006).

Epps, D.E., Sarver, R.W., Rogers, J.M., Herberg, J.T. & Tomich, P.K. The ligand affinity of proteins measured by isothermal denaturation kinetics. Anal. Biochem. 292, 40–50 (2001).

Plotnikov, V. et al. An autosampling differential scanning calorimeter instrument for studying molecular interactions. Assay Drug Dev. Technol. 1 1 (Part 1): 83–90 (2002).

Pace, C.N., Vajdos, F., Fee, L., Grimsley, G. & Gray, T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411–2423 (1995).

Greenfield, N.J. Using circular dichroism spectra to estimate protein secondary structure. Nat. Protoc. 1, 2876–2890 (2006).

Dawson, R.M.C., Elliott, D.C., Elliott, W.H. & Jones, K.M. Data for Biochemical Research 3rd edn. (Oxford University Press, Oxford, UK, 1986).