Production of correctly folded recombinant [13C, 15N]-enriched guinea pig [Val90]-α-lactalbumin

Protein Engineering

Volumn 10, Issue 4, 1997, Pages 455-462

  Kim, Seho ^a   Baum, Jean ^b   Anderson, Stephen ^b,c  

^a UNIVERSITY OF MEDICINE AND DENTISTRY OF NEW JERSEY   (United States)

^b RUTGERS UNIVERSITY   (United States)

^c RUTGERS UNIVERSITY   (United States)

Author keywords

Guinea pig; Recombinant lactalbumin

Indexed keywords

ALPHA LACTALBUMIN; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CELL INCLUSION; CIRCULAR DICHROISM; ESCHERICHIA COLI; GENE FUSION; GENETIC ENGINEERING; GUINEA PIG; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SYNTHESIS; PROTON NUCLEAR MAGNETIC RESONANCE;

ANIMALS; CIRCULAR DICHROISM; GUINEA PIGS; LACTALBUMIN; MAGNETIC RESONANCE SPECTROSCOPY; MASS SPECTROMETRY; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT PROTEINS; VALINE;

CAVIA PORCELLUS; ESCHERICHIA COLI; SUS SCROFA;

EID: 0031007198     PISSN: 02692139     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (46)

1. Acharya, K.R., Stuart, D.I., Walker, N.P.C., Lewis, M. and Phillips, D.C. (1989) J. Mol. Biol., 208, 99-127.
2. Acharya, K.R., Ren, J., Stuart, D.I., Phillips, D.C. and Fenna, R.E. (1991) J. Mol. Biol., 221, 571-581.
3. Alexandrescu, A.T., Evans, P.A., Pitkeathly, M., Baum, J. and Dobson, C.M. (1993) Biochemistry, 32, 1707-1718.
4. Altman, J.D., Henner, D., Nilsson, B., Anderson, S. and Kuntz, I. (1991) Protein Engng, 4, 593-600.
5. Baum, J., Dobson, C.M., Evans, P.A. and Hanley, C. (1989) Biochemistry, 28, 7-13.
6. Bax, A., Ikura, M., Kay, L.E., Tochia, D.A. and Tschudin, R. (1990) J. Magn. Reson., 86, 304-318.
7. Chyan, C., Wormald, C., Dobson, C.M., Evans, P.A. and Baum, J. (1993) Biochemistry, 32, 5681-5691.
8. Damaschun, G., Gernat, C., Damaschun, H., Bychkova, V.E. and Ptitsyn, O.B. (1986) Int. J. Biol. Macromol., 8, 226-230.
9. Davis, A., Keeler, J., Laue, E.D. and Moskau, D. (1992) J. Magn. Reson., 98, 207-216.
10. Dobson, C.M. (1994) Curr. Biol., 4, 636-640.
11. Dolgikh, D.A., Gilmanshin, R.I., Brazhnikov, E.V., Bychkova, V.E., Semisotnov, G.V., Venyaminov, S.Y. and Ptitsyn, O.B. (1981) FEBS Lett., 136, 311-315.
12. Ernst, R.R., Bodenhausen, G. and Wokaun, A. (1987) Principles of Nuclear Magnetic Resonance in One and Two Dimensions. Oxford University Press, New York, pp. 317-322 and 516-527.
13. Ewbank, J.J. and Creighton, T.E. (1991) Nature, 350, 518-520.
14. Ewbank, J.J. and Creighton, T.E. (1993) Biochemistry, 32, 3677-3693.
15. Fitzgerald, D.K., Colvin, B., Mawal, R. and Ebner, K.E. (1970) Anal. Biochem., 36, 43-61.
16. Goldberg, M.E., Rudolph, R. and Jaenicke, R. (1991) Biochemistry, 30, 2790-2797.
17. Griko, Y.V., Freire, E. and Privalov, P.L. (1994) Biochemistry, 33, 1889-1899.
18. Grobler, J.A., Wang, M., Pike, A.C.W. and Brew, K. (1994) J. Biol. Chem., 269, 5106-5114.
19. Gross, E. (1967) Methods Enzymol., 11, 238-255.
20. Hall, L., Craig, R.K., Edbrooke, M.R. and Campbell, P.N. (1982) Nucleic Acids Res., 10, 3503-3515.
21. Hölpert, M. and Cooper, T.G. (1990) Anal. Biochem., 188, 168-175.
22. Jansson, M., Li, Y.C., Jendeberg, L., Anderson, S., Montelione, G.T. and Nilsson, B. (1996) J. Biomol. NMR, 7, 131-141.
23. Kronman, M., Sinha, S.K. and Brew, K. (1981) J. Biol. Chem., 256, 8582-8587.
24. Kumagai, I., Takeda, S., Hibino, T. and Miura, K. (1990) Protein Engng, 3, 449-452.
25. Kuwajima, K. (1989) Proteins: Struct. Funct. Genet., 6, 87-103.
26. Kuwajima, K., Hiraoka, Y., Ikeguchi, M. and Sugai, S. (1985) Biochemistry, 24, 874-881.
27. Kuwajima, K., Harushima, Y. and Sugai, S. (1986) Int. J. Pept. Protein Res., 27, 18-27.
28. Laird, J.E., Jack, L., Hall, L., Boulton, A.P., Parker, D. and Craig, R.K. (1988) Biochem. J., 254, 85-94.
29. Lindahl, L. and Vogel, H.J. (1984) Anal. Biochem., 140, 394-402.
30. Marion, D., Kay, L.E., Sparks, S.W., Torchia, D.A. and Bax, A. (1989) J. Am. Chem. Soc., 111, 1515-1517.
31. McKenzie, H.A. and White, J.F.H. (1991) Adv. Protein Chem., 41, 173-315.
32. Murakami, K., Andree, P.J. and Berliner, L.J. (1982) Biochemistry, 21, 5488-5494.
33. Neuhaus, D. and Williamson, M. (1989) The Nuclear Overhauser Effect in Structural and Conformational Analysis. VCH, New York, pp. 253-305.
34. Nilsson, B. and Abrahmśen, L. (1990) Methods Enzymol., 185, 144-161.
35. Peng, Z. and Kim, P.S. (1994) Biochemistry, 33, 2136-2141.
36. Peng, Z., Wu, L.C. and Kim, P.S. (1995) Biochemistry, 34, 3248-3252.
37. Ptitsyn, O.B. (1995) Curr. Opin. Struct. Biol., 5, 74-78.
38. Ptitsyn, O.B., Pain, R.H., Semisotnov, G.V., Zerovnik, E. and Razgulgaev, O.I. (1990) FEBS Lett., 262, 20-24.
39. Rao, K.R. and Brew, K. (1989) Biochem. Biophys. Res. Commun., 163, 1390-1396.
40. Sanger, F., Nicklen, S. and Coulson, A.R. (1977) Proc. Natl Acad. Sci. USA, 74, 5463-5467.
41. Schulman, B.A., Redfield, C., Peng, Z., Dobson, C.M. and Kim, P.S. (1995) J. Mol. Biol., 253, 651-657.
42. Thannhauser, T.W., Konishi, Y. and Scheraga, H.A. (1987) Methods Enzymol., 143, 115-119.
43. Viaene, A., Volckaert, G., Joniau, M., De Baetselier, A. and Van Cauwelaert, F. (1991) Eur. J. Biochem., 202, 471-477.
44. Vuister, G.W. and Bax, A. (1992) J. Magn. Reson., 98, 428-435.
45. Wang, M., Scott, W.A., Rao, K.R., Udey, J., Conner, G.E. and Brew, K. (1989) J. Biol. Chem., 264, 21116-21121.
46. Wu, L.C., Peng, Z. and Kim, P.S. (1995) Nature Struct. Biol., 2, 281-286.