Effects of positively charged redox molecules on disulfide-coupled protein folding

FEBS Letters

Volumn 586, Issue 21, 2012, Pages 3926-3930

  Okumura, Masaki ^a,b   Shimamoto, Shigeru ^a   Nakanishi, Takeyoshi ^a   Yoshida, Yu Ichiro ^a   Konogami, Tadafumi ^a   Maeda, Shogo ^a   Hidaka, Yuji ^a  

^a KINKI UNIVERSITY   (Japan)

^b KWANSEI GAKUIN UNIVERSITY   (Japan)

Author keywords

Disulfide; Folding; Glutathione; Intermediate; Lysozyme; Prouroguanylin; Thiol

Indexed keywords

3 MERCAPTOPROPIONIC ACID; CYSTEINE; DISULFIDE; GLUTATHIONE; LYSOZYME; MERCAPTAMINE; MERCAPTOETHANOL; PROUROGUANYLIN; THIOL DERIVATIVE; UNCLASSIFIED DRUG; UROGUANYLIN;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; DISULFIDE COUPLED PROTEIN FOLDING; MOLECULAR SIZE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; SURFACE CHARGE;

CHROMATOGRAPHY, REVERSE-PHASE; DISULFIDES; GLUTATHIONE; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MURAMIDASE; OXIDATION-REDUCTION; PROTEIN FOLDING; PROTEIN PRECURSORS; SOLUTIONS; STATIC ELECTRICITY; SULFHYDRYL COMPOUNDS;

EID: 84868125703     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2012.09.031     Document Type: Article

References (28)

1. C.B. Anfinsen Principles that govern the folding of protein chains Science 181 1973 223 230
2. T.R. Sosnick, and D. Barrick The folding of single domain proteins-have we reached a consensus? Curr. Opin. Struct. Biol. 21 2011 12 24
3. Y. Hidaka Disulfide-coupled protein folding: looking back, looking forward FEBS J. 279 2012 2261
4. Y. Sato, and K. Inaba Disulfide bond formation network in the biological kingdoms FEBS J. 279 2012 2262 2271
5. M. Narayan Disulfide bonds: protein folding and subcellular protein trafficking FEBS J. 279 2012 2272 2282
6. Y. Konishi, T. Ooi, and H.A. Scheraga Regeneration of ribonuclease A from the reduced protein. Rate-limiting steps Biochemistry 21 1982 4734 4740
7. F.M. Kibria, and W.J. Lees Balancing conformational and oxidative kinetic traps during the folding of bovine pancreatic trypsin inhibitor (BPTI) with glutathione and glutathione disulfide J. Am. Chem. Soc. 130 2008 796 797
8. J.L. Arolas, D. Pantoja-Uceda, S. Ventura, F.J. Blanco, and F.X. Aviles The NMR structures of the major intermediates of the two-domain tick carboxypeptidase inhibitor reveal symmetry in its folding and unfolding pathways J. Biol. Chem. 283 2008 27110 27120
9. a effects on the folding rate of a disulfide containing protein Biochemistry 42 2003 11787 11797
10. J. Beld, K.J. Woycechowsky, and D. Hilvert Selenoglutathione: efficient oxidative protein folding by a diselenide Biochemistry 46 2007 5382 5390
11. M. Okumura, M. Saiki, H. Yamaguchi, and Y. Hidaka Acceleration of disulfide-coupled protein folding using glutathione derivatives FEBS J. 278 2011 1137 1144
12. M. Okumura, S. Shimamoto, and Y. Hidaka A chemical method for investigating disulfide-coupled peptide and protein folding FEBS J. 279 2012 2283 2295
13. Y. Hidaka, M. Ohno, B. Hemmasi, O. Hill, W.G. Forssmann, and Y. Shimonishi In vitro disulfide-coupled folding of guanylylcyclase-activating peptide and its precursor protein Biochemistry 37 1998 8498 8507
14. B. Raman, T. Ramakrishna, and C.M. Rao Refolding of denatured and denatured/reduced lysozyme at high concentrations J. Biol. Chem. 271 1996 17067 17072
15. V.P. Saxena, and D.B. Wetlaufer Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme Biochemistry 9 1970 5015 5023
16. M. Kudou, K. Shiraki, S. Fujiwara, T. Imanaka, and M. Takagi Prevention of thermal inactivation and aggregation of lysozyme by polyamines Eur. J. Biochem. 270 2003 4547 4554
17. W.J. Wedemeyer, E. Welker, M. Narayan, and H.A. Scheraga Disulfide bonds and protein folding Biochemistry 39 2000 4207 4216
18. L. Moroder, D. Besse, H.J. Musiol, S. Rudolph-Bohner, and F. Siedler Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies Biopolymers 40 1996 207 234
19. S. Chakravarthi, C.E. Jessop, and N.J. Bulleid The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress EMBO Rep. 7 2006 271 275
20. a, and thiol concentration J. Biotechnol. 115 2005 279 290
21. M.M. Wu, M. Grabe, S. Adams, R.Y. Tsien, H.P. Moore, and T.E. Machen Mechanisms of pH regulation in the regulated secretory pathway J. Biol. Chem. 276 2001 33027 33035
22. M. Friedman, J.F. Cavins, and J.S. Wall Relative nucleophilic reactivities of amino groups and mercaptide ions in addition reactions with α,β-unsaturated compounds J. Am. Chem. Soc. 87 1965 3672 3682
23. J.T. Edsall, and J. Wyman Biophysical Chemistry 1958 Academic Press Inc. New York
24. H. Lindley A study of the kinetics of the reaction between thiol compounds and choloracetamide Biochem. J. 74 1960 577 584
25. G.J. Buist, and H.J. Lucas Basicity constants and rates of hydration of some imines J. Am. Chem. Soc. 79 1957 6157 6160
26. V. Franzen Beziehungen Zwischen Konstitution und Katalytischer Aktivität von Thiolaminen Bei der Katalyse der Intramolekularen Cannizzaro-Reaktion Chem. Ber. 90 1957 623 633
27. G.H. Snyder, M.J. Cennerazzo, A.J. Karalis, and D. Field Electrostatic influence of local cysteine environments on disulfide exchange kinetics Biochemistry 20 1981 6509 6519
28. F. Csizmadia JChem: java applets and modules supporting chemical database handling from web browsers J. Chem. Inf. Comput. Sci. 40 2000 323 324