Rhodanese folding is controlled by the partitioning of its folding intermediates

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1382, Issue 1, 1998, Pages 120-128

  Gorovits, Boris M ^a   McGee, William A ^a   Horowitz, Paul M ^a  

^a UNIVERSITY OF TEXAS HEALTH SCIENCE CENTER AT SAN ANTONIO   (United States)

Author keywords

Folding intermediates; Glycerol protein stabilization; Protein folding; Rhodanese

Indexed keywords

CHAPERONIN; GLYCEROL; THIOSULFATE SULFURTRANSFERASE;

ARTICLE; CATTLE; CONTROLLED STUDY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; RENATURATION; TEMPERATURE DEPENDENCE;

ANIMALS; CATTLE; ENZYME STABILITY; GLYCEROL; GROEL PROTEIN; KINETICS; MODELS, CHEMICAL; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS; THIOSULFATE SULFURTRANSFERASE; UREA;

BOS TAURUS; BOVINAE;

EID: 0031890719     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(97)00158-1     Document Type: Article

References (20)

1. P.M. Horowitz, in: M.E. Himmel, G. Georgiou (Ed.), Biocatalyst Design for Stability and Specificity, ACS Symposium Series No.516, 1993.
2. Mendoza J.A., Rogers E., Lorimer G.H., Horowitz P.M. J. Biol. Chem. 266:1991;13044-13049.
3. Ploegman J.H., Drent G., Kalk K.H., Hol W.G.J., Heinrikson R.L., Keim P., Weng L., Russel J. Nature. 273:1978;124-129.
4. Mendoza J.A., Rogers E., Lorimer G.H., Horowitz P.M. J. Biol. Chem. 266:1991;13587-13591.
5. Tandon S., Horowitz P.M. J. Biol. Chem. 264:1989;9859-9866.
6. Schumann J., Mollering H., Jaenicke R. Biol.Chem. Hoppe-Seyler. 374:1993;427-434.
7. Miller D.M., Delgado R., Chirgwin J.M., Hardies S.C., Horowitz P.M. J. Biol. Chem. 266:1991;4686-4691.
8. Sörbo B.H. Acta Chem. Scand. 7:1953;1129-1136.
9. Pace N. Trends Biotechnol. 8:1990;93-98.
10. van Holde K.E., Weishet W.O. Biopolymers. 17:1978;1387-1403.
11. Gorovits B.M., Seale J.W., Horowitz P.M. Biochemistry. 34:1995;13928-13933.
12. Horowitz P.M., Criscimagna N.L. J. Biol. Chem. 265:1990;2576-2583.
13. Horowitz P.M., Butler M. J. Biol. Chem. 268:1993;2500-2504.
14. Schultes V., Jaenicke R. FEBS. 290:1991;235-238.
15. Oliveira A.C., Gaspar L.P., Da Poian A.T., Silva J.L. J. Mol. Biol. 240:1994;184-187.
16. Amir D., Krausz S., Haas E. Proteins. 13:1992;162-173.
17. S.N. Timasheff, in: B.A. Shirley (Ed.), Methods in Molecular Biology, vol. 40, Humana Press Inc., Totowa, NJ, 1995, pp. 253-269.
18. Chrunyc B.A., Matthews C.R. Biochemistry. 29:1990;2149-2154.
19. Xie Y., Wetlaufer D.B. Protein Sci. 5:1996;517-523.
20. Tachibana H., Ohta K., Sawano H., Koumoto Y., Segawa S. Biochemistry. 33:1994;15008-15016.