Gas-phase processes and measurements of macromolecular properties in solution: On the possibility of false positive and false negative signals of protein unfolding

International Journal of Mass Spectrometry

Volumn 253, Issue 3, 2006, Pages 207-216

  Abzalimov, Rinat R ^a   Frimpong, Agya K ^a   Kaltashov, Igor A ^a  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

Asymmetric dissociation; Charge state distribution; Electrospray ionization; Non covalent complex; Proton affinity

Indexed keywords

EID: 33745285701     PISSN: 13873806     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijms.2006.03.002     Document Type: Article

References (40)

1. Kaltashov I.A., and Eyles S.J. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom. Rev. 21 (2002) 37
2. Kaltashov I.A., and Eyles S.J. Mass Spectrometry in Molecular Biophysics: Conformation and Dynamics of Biomolecules (2005), John Wiley, Hoboken, NJ
3. Engen J.R., and Smith D.L. Investigating protein structure and dynamics by hydrogen exchange MS. Anal. Chem. 73 (2001) 256A
4. Hoofnagle A.N., Resing K.A., and Ahn N.G. Protein analysis by hydrogen exchange mass spectrometry. Annu. Rev. Biophys. Biomol. Struct. 32 (2003) 1
5. Wolynes P.G. Biomolecular Folding in Vacuo?. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 2426
6. Kaltashov I.A., and Eyles S.J. Crossing the phase boundary to study protein dynamics and function: combination of amide hydrogen exchange in solution and ion fragmentation in the gas phase. J. Mass Spectrom. 37 (2002) 557
7. Hoerner J.K., Xiao H., Dobo A., and Kaltashov I.A. Is there hydrogen scrambling in the gas phase? Energetic and structural determinants of proton mobility within protein ions. J. Am. Chem. Soc. 126 (2004) 7709
8. Peschke M., Verkerk U.H., and Kebarle P. Features of the ESI mechanism that affect the observation of multiply charged non-covalent protein complexes and the determination of the association constant by the titration method. J. Am. Soc. Mass Spectrom. 15 (2004) 1424
9. Konermann L., and Douglas D.J. Equilibrium unfolding of proteins monitored by electrospray ionization mass spectrometry: distinguishing two-state from multi-state transitions. Rapid Commun. Mass Spectrom. 12 (1998) 435
10. Dobo A., and Kaltashov I.A. Detection of multiple protein conformational ensembles in solution via deconvolution of charge state distributions in ESI MS. Anal. Chem. 73 (2001) 4763
11. Chowdhury S.K., Katta V., and Chait B.T. Probing conformational changes in proteins by mass spectrometry. J. Am. Chem. Soc. 112 (1990) 9012
12. Mohimen A., Dobo A., Hoerner J.K., and Kaltashov I.A. A chemometric approach to detection and characterization of multiple protein conformers in solution using electrospray ionization mass spectrometry. Anal. Chem. 75 (2003) 4139
13. Kaltashov I.A., and Mohimen A. Estimates of protein surface areas in solution by electrospray ionization mass spectrometry. Anal. Chem. 77 (2005) 5370
14. Gumerov D.R., Dobo A., and Kaltashov I.A. Protein-ion charge-state distributions in electrospray ionization mass spectrometry: distinguishing conformational contributions from masking effects. Eur. J. Mass Spectrom. 8 (2002) 123
15. Chernushevich I.V., and Thomson B.A. Collisional cooling of large ions in electrospray mass spectrometry. Anal. Chem. 76 (2004) 1754
16. Loo J.A. Electrospray ionization mass spectrometry: a technology for studying non-covalent macromolecular complexes. Int. J. Mass Spectrom. 200 (2000) 175
17. Heck A.J., and Van Den Heuvel R.H. Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. 23 (2004) 368
18. Dobson C.M. Principles of protein folding, misfolding and aggregation. Semin. Cell Dev. Biol. 15 (2004) 3
19. 19 alloform. J. Am. Chem. Soc. 127 (2005) 2075
20. 2-microglobulin uncovered quantitatively by electrospray ionization mass spectrometry. J. Biol. Chem. 279 (2004) 27069
21. 2-microglobulin. Biochemistry 44 (2005) 4397
22. Donovan M., Olofsson B., Gustafson A.L., Dencker L., and Eriksson U. The cellular retinoic acid binding proteins. J. Steroid Biochem. Mol. Biol. 53 (1995) 459
23. Krishnan V.V., Sukumar M., Gierasch L.M., and Cosman M. Dynamics of cellular retinoic acid binding protein I on multiple time scales with implications for ligand binding. Biochemistry 39 (2000) 9119
24. Jurchen J.C., Garcia D.E., and Williams E.R. Gas-phase dissociation pathways of multiply charged peptide clusters. J. Am. Soc. Mass Spectrom. 14 (2003) 1373
25. Jurchen J.C., and Williams E.R. Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers. J. Am. Chem. Soc. 125 (2003) 2817
26. Schwartz B.L., Bruce J.E., Anderson G.A., Hofstadler S.A., Rockwood A.L., Smith R.D., Chilkoti A., and Stayton P.S. Dissociation of tetrameric ions of non-covalent streptavidin complexes formed by electrospray-ionization. J. Am. Soc. Mass Spectrom. 6 (1995) 459
27. Sobott F., McCammon M.G., and Robinson C.V. Gas-phase dissociation pathways of a tetrameric protein complex. Int. J. Mass Spectrom. 230 (2003) 193
28. Felitsyn N., Kitova E.N., and Klassen J.S. Thermal decomposition of a gaseous multiprotein complex studied by blackbody infrared radiative dissociation. Investigating the origin of the asymmetric dissociation behavior. Anal. Chem. 73 (2001) 4647
29. Jurchen J.C., Garcia D.E., and Williams E.R. Further studies on the origins of asymmetric charge partitioning in protein homodimers. J. Am. Soc. Mass Spectrom. 15 (2004) 1408
30. Csiszar S., and Thachuk M. Using ellipsoids to model charge distributions in gas phase protein complex ion dissociation. Can. J. Chem. 82 (2004) 1736
31. Seidl M., and Brack M. Liquid drop model for charged spherical metal clusters. Ann. Phys. 245 (1996) 275
32. de la Mora J.F. Electrospray ionization of large multiply charged species proceeds via Dole's charged residue mechanism. Anal. Chim. Acta 406 (2000) 93
33. de la Mora J.F. On the outcome of the coulombic fission of a charged isolated drop. J. Coll. Int. Sci. 178 (1996) 209
34. Ryce S.A., and Wyman R.R. Asymmetry in electrostatic dispersion of liquids. Can. J. Phys. 42 (1964) 2185
35. Manning J.M., Dumoulin A., Li X., and Manning L.R. Normal and abnormal protein subunit interactions in hemoglobins. J. Biol. Chem. 273 (1998) 19359
36. Peschke M., Verkerk U.H., and Kebarle P. Prediction of the charge states of folded proteins in electrospray ionization. Eur. J. Mass Spectrom. 10 (2004) 993
37. Schnier P.D., Gross D.S., and Williams E.R. On the maximum charge state and proton transfer reactivity of peptide and protein ions formed by electrospray ionization. J. Am. Soc. Mass Spectrom. 6 (1995) 1086
38. Andreeva N.S. How and why is pepsin stable and active at pH 2?. Mol. Biol. (Mosk.) 28 (1994) 1400
39. Campos L.A., and Sancho J. The active site of pepsin is formed in the intermediate conformation dominant at mildly acidic pH. FEBS Lett. 538 (2003) 89
40. Vonhelden G., Wyttenbach T., and Bowers M.T. Conformation of macromolecules in the gas phase. Science 267 (1995) 1483