Trimethylamine-N-oxide modulates the reductive unfolding of onconase

Biochemical and Biophysical Research Communications

Volumn 325, Issue 3, 2004, Pages 707-710

  Gahl, Robert F ^a   Narayan, Mahesh ^a   Xu, Guoqiang ^a   Scheraga, Harold A ^a  

^a Department of Molecular Biology and Genetics   (United States)

Author keywords

Free energy; Onconase; Osmolyte; Reductive unfolding; TMAO

Indexed keywords

RANPIRNASE; TRIMETHYLAMINE OXIDE;

ARTICLE; DENATURATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; REDUCTION;

ENZYME INHIBITORS; ENZYME STABILITY; METHYLAMINES; OXIDATION-REDUCTION; PROTEIN CONFORMATION; PROTEIN DENATURATION; RIBONUCLEASES;

EID: 8444249624     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.10.088     Document Type: Article

References (20)

1. A. Wang, and D.W. Bolen A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation Biochemistry 36 1997 9101 9108
2. I. Baskakov, and D.W. Bolen Forcing thermodynamically unfolded proteins to fold J. Biol. Chem. 273 1998 4831 4834
3. D.S. Yang, C.M. Yip, T.H. Huang, A. Chakrabartty, and P.E. Fraser Manipulating the amyloid-β aggregation pathway with chemical chaperones J. Biol. Chem. 274 1999 32970 32974
4. 1H NMR studies of the effect of the counteracting osmolyte trimethylamine-N-oxide on interactions of urea with ribonuclease A J. Biol. Chem. 275 2000 27708 27711
5. V.N. Uversky, J. Li, and A.L. Fink Trimethylamine-N-oxide-induced folding of α-synuclein FEBS Lett. 509 2001 31 35
6. D.K. Eggers, and J.S. Valentine Crowding and hydration effects on protein conformation: a study with sol-gel encapsulated proteins J. Mol. Biol. 314 2001 911 922
7. G.S. Ratnaparkhi, and R. Varadarajan Osmolytes stabilize ribonuclease S by stabilizing its fragments S protein and S peptide to compact folding-competent states J. Biol. Chem. 276 2001 28789 28798
8. S.A. Celinski, and J.M. Scholtz Osmolyte effects on helix formation in peptides and the stability of coiled-coils Protein Sci. 11 2002 2048 2051
9. P.H. Yancey, W.R. Blake, and J. Conley Unusual organic osmolytes in deep-sea animals: adaptations to hydrostatic pressure and other perturbants J. Comp. Biochem. Physiol. Part A 133 2002 667 676
10. Q. Zou, B.J. Bennion, V. Daggett, and K.P. Murphy The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea J. Am. Chem. Soc. 124 2002 1192 1202
11. Y. Qu, and D.W. Bolen Hydrogen exchange kinetics of RNase A and the urea: TMAO paradigm Biochemistry 42 2003 5837 5849
12. B.J. Bennion, and V. Daggett Counteraction of urea-induced protein denaturation by trimethylamine-N-oxide: a chemical chaperone at atomic resolution Proc. Natl. Acad. Sci. USA 101 2004 6433 6438
13. M. Auton, and D.W. Bolen Additive transfer free energies of the peptide backbone unit that are independent of the model compound and the choice of concentration scale Biochemistry 43 2004 1329 1342
14. L. Pradeep, and J.B. Udgaonkar Osmolytes induce structure in an early intermediate on the folding pathway of barstar J. Biol. Chem. 279 2004 40303 40313
15. S.C. Mosimann, W. Ardelt, and M.N. James Refined 1.7 Å X-ray crystallographic structure of P-30 protein, an amphibian ribonuclease with anti-tumor activity J. Mol. Biol. 236 1994 1141 1153
16. Y.J. Li, D.M. Rothwarf, and H.A. Scheraga Mechanism of reductive protein unfolding Nat. Struct. Biol. 2 1995 489 494
17. G. Xu, M. Narayan, E. Welker, and H.A. Scheraga Characterization of the fast-forming intermediate, des [30-75], in the reductive unfolding of onconase Biochemistry 43 2004 3246 3254
18. M. Narayan, G. Xu, D.R. Ripoll, H. Zhai, K. Breuker, C. Wanjalla, H.J. Leung, A. Navon, E. Welker, F.W. McLafferty, and H.A. Scheraga Dissimilarity in the reductive unfolding pathways of two ribonuclease homologues J. Mol. Biol. 338 2004 795 809
19. D.M. Rothwarf, and H.A. Scheraga Equilibrium and kinetic constants for the thiol-disulfide interchange reaction between glutathione and dithiothreitol Proc. Natl. Acad. Sci. USA 89 1992 7944 7948
20. H.J. Leung, G. Xu, M. Narayan, H.A. Scheraga, Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide- containing proteins, J. Pep. Res. (in press)