Refolding out of guanidine hydrochloride is an effective approach for high-throughput structural studies of small proteins

Protein Science

Volumn 12, Issue 9, 2003, Pages 2073-2080

  Maxwell, Karen L ^a   Bona, Diane ^a   Liu, Chengsong ^a   Arrowsmith, Cheryl H ^a   Edwards, Aled M ^b  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

Circular dichroism spectroscopy; NMR spectroscopy; Protein purification; Protein solubility; Protein structure folding; Structural proteomics

Indexed keywords

ARCHAEAL PROTEIN; BACTERIAL PROTEIN; GUANIDINE; RECOMBINANT PROTEIN;

ARTICLE; DIALYSIS; ESCHERICHIA COLI; GENE OVEREXPRESSION; HETERONUCLEAR SINGLE QUANTUM COHERENCE NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; IN VIVO STUDY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEOMICS; REACTION OPTIMIZATION; SOLUBILITY; X RAY CRYSTALLOGRAPHY;

BIOPHYSICS; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GUANIDINE; MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; PROTEOME; PROTEOMICS; RECOMBINANT PROTEINS;

ARCHAEA; BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0042510932     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0393503     Document Type: Article

References (15)

1. Babbitt, P.C., West, B.L., Buechter, D.D., Kuntz, I.D., and Kenyon, G.L. 1990. Removal of a proteolytic activity associated with aggregates formed from expression of creatine kinase in Escherichia coli leads to improved recovery of active enzyme. Biotechnology 8: 945-949.
2. Blattner, F.R., Plunkett III, G., Bloch, C.A., Perna, N.T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J.D., Rode, C.K., Mayhew, G.F., et al. 1997. The completed genome sequence of Escherichia coli K-12. Science 277: 1453-1474.
3. Christendat, D., Yee, A., Dharamsi, A., Kluger, Y., Gerstein, M., Arrowsmith, C.H., and Edwards, A.M. 2000a. Structural proteomics: Prospects for high throughput sample preparation. Prog. Biophys. Mol. Biol. 73: 339-345.
4. Christendat, D., Yee, A., Dharamsi, A., Kluger, Y., Savchenko, A., Cort, J.R., Booth, V., Mackereth, C.D., Saridakis, V., Ekiel, I., et al. 2000b. Structural proteomics of an archaeon. Nat. Struct. Biol. 7: 903-909.
5. Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. 1995. NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 4: 603-614.
6. Goffeau, A., Barrell, B.G., Bussey, H., Davis, R.W., Dujon, B., Feldmann, H., Galibert, F., Hoheisel, J.D., Jacq, C., Johnston, M., et al. 1996. Life with 6000 genes. Science 274: 563-567.
7. Hammarstrom, M., Hellgren, N., van Den Berg, S., Berglund, H., and Hard, T. 2002. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 11: 313-321.
8. Maachupalli-Reddy, J., Kelley, B.D., and De Bernardez Clark, E. 1997. Effect of inclusion body contaminants on the oxidative renaturation of hen egg white lysozyme. Biotechnol. Prog. 13: 144-150.
9. Nelson, K., Clayton, R.A., Gill, S.R., Gwinn, M.L., Dodson, R.J., Haft, D.H., Hickey, E.K., Peterson, J.D., Nelson, W.C., Ketchum, K.A., et al. 1999. Evidence for lateral gene transfer between archaea and bacteria from genome sequence of Thermotoga maritima. Nature 399: 323-329.
10. Savchenko, A., Yee, A., Khachatryan, A., Skarina, T., Evdokimova, E., Pavlova, M., Semesi, A., Northey, J., Beasley, S., Lan, N., et al. 2003. Strategies for structural proteomics of prokaryotes: Quantifying the advantages of studying orthologous proteins and of using both NMR and X-ray crystallography approaches. Proteins 15: 392-399.
11. Shih, Y.P., Kung, W.M., Chen, J.C., Yeh, C.H., Wang, A.H., and Wang, T.F. 2002. High-throughput screening of soluble recombinant proteins. Protein Sci. 11: 1714-1719.
12. Smith, D.R., Doucette-Stamm, L.A., Deloughery, C., Lee, H., Dubois, J., Aldredge, T., Bashirzadeh, R., Blakely, D., Cook, R., Gilbert, K., et al. 1997. Complete genome sequence of Methanobacterium thermoautotrophicum δH: Functional analysis and comparative genomics. J. Bacteriol. 179: 7135-7155.
13. Tran-Moseman, A., Schauer, N., and De Bernardez Clark, E. 1999. Renaturation of Escherichia coli-derived recombinant human macrophage colony-stimulating factor. Protein Expr. Purif. 16: 181-189.
14. Wong, H.H., O'Neill, B.K., and Middelberg, A.P. 1996. Centrifugal recovery and dissolution of recombinant Gly-IGF-II inclusion-bodies: The impact of feedrate and re-centrifugation on protein yield. Bioseparation 6: 185-192.
15. Yee, A., Chang, X., Pineda-Lucena, A., Wu, B., Semesi, A., Le, B., Ramelot, T., Lee, G.M., Bhattacharyya, S., Gutierrez, P., et al. 2002. An NMR approach to structural proteomics. Proc. Natl. Acad. Sci. 99: 1825-1830.