Using ESI-MS to Probe Protein Structure by Site-Specific Noncovalent Attachment of 18-Crown-6

Journal of the American Society for Mass Spectrometry

Volumn 17, Issue 9, 2006, Pages 1209-1215

  Ly, Tony ^a   Julian, Ryan R ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE STATE; EQUILIBRIUM STRUCTURES; INTRAMOLECULAR INTERACTIONS; PENTALYSINE;

ETHERS; IONIZATION; MASS SPECTROMETRY; MICROORGANISMS; MOLECULAR ORIENTATION; ORGANIC SOLVENTS;

PROTEINS;

CROWN COMPOUND; CYTOCHROME C; LYSINE; MELITTIN; ORGANIC SOLVENT; PROTEIN; UBIQUITIN;

ARTICLE; COVALENT BOND; ELECTROSPRAY MASS SPECTROMETRY; EQUILIBRIUM CONSTANT; MOLECULAR INTERACTION; MOLECULAR PROBE; PH; PH MEASUREMENT; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SENSITIVITY ANALYSIS; SOLVENT EFFECT; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BINDING SITES; CROWN ETHERS; MOLECULAR PROBE TECHNIQUES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN INTERACTION MAPPING; PROTEINS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; STAINING AND LABELING;

EID: 33747882757     PISSN: 10440305     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jasms.2006.05.007     Document Type: Article

References (35)

1. Wales T.E., and Engen J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev 25 (2006) 158-170
2. Kaltashov I.A., and Eyles S.J. Studies of biomolecular conformations and conformational dynamics by mass spectrometry. Mass Spectrom. Rev 21 (2002) 37-71
3. Englander S.W. Protein folding intermediates and pathways studied by hydrogen exchange. Annu. Rev. Biophys. Biomol. Struct 29 (2000) 213-238
4. Mandell J.G., Falick A.M., and Komives E.A. Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry. Anal. Chem 70 (1998) 3987-3995
5. Garcia R.A., Pantazatos D., and Villareal F.J. Hydrogen/deuterium exchange mass spectrometry for investigating protein-ligand interactions. Assay Drug Dev. Technol 2 (2004) 81-91
6. Zhu M.M., Chitta R., and Gross M.L. PLIMSTEX. A novel mass spectrometric method for the quantification of protein-ligand interactions in solution. Int. J. Mass Spectrom 240 (2005) 213-220
7. Roulhac P.L., Powell K.D., Dhungana S., Weaver K.D., Mietzner T.A., Crumbliss A.L., and Fitzgerald M.C. SUPREX (stability of unpurified proteins from rates of H/D exchange) analysis of the thermodynamics of synergistic anion binding by ferric-binding protein (FbpA), a bacterial transferrin. Biochemistry 43 (2004) 15767-15774
8. Pan J., Wilson D.J., and Konermann L. Pulsed hydrogen exchange and electrospray charge-state distribution as complementary probes of protein structure in kinetic experiments. Implications for ubiquitin folding. Biochemistry 44 (2005) 8627-8633
9. Yan X., Watson J., Ho P.S., and Deinzer M.L. Mass spectrometric approaches using electrospray ionization charge states and hydrogen-deuterium exchange for determining protein structures and their conformational changes. Mol. Cell. Proteom 3 (2003) 10-23
10. Grandori R. Origin of the conformation dependence of protein charge-state distributions in electrospray ionization mass spectrometry. J. Mass Spectrom 38 (2003) 11-15
11. 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) 4763-4773
12. Fenn J.B. Ion formation from charged droplets-roles of geometry, energy, and time. J. Am. Soc. Mass Spectrom 4 (1993) 524-535
13. 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) 435-442
14. Konermann L., and Douglas D.J. Unfolding of proteins monitored by electrospray ionization mass spectrometry. A comparison of positive and negative ion modes. J. Am. Soc. Mass Spectrom 9 (1998) 1248-1254
15. Julian R.R., and Beauchamp J.L. Site specific sequestering and stabilization of charge in peptides by supramolecular adduct formation with 18-crown-6 ether by way of electrospray ionization. Int. J. Mass Spectrom 210 (2001) 613-623
16. Cunniff J.B., and Vouros P. Mass and charge state assignment for proteins and peptide mixtures via noncovalent adduction in electrospray mass spectrometry. J. Am. Soc. Mass Spectrom 6 (1995) 1175-1182
17. Sproch N., and Kruger T.L. Noncovalent interactions of crown ethers with cytochrome c using electrospray mass spectrometry (1993) 904a-904b Proceedings of the 41st ASMS Conference; San Francisco, CA
18. Bosch E., Bou P., Allemann H., and Rosès M. Retention of ionizable compounds on HPLC. pH scale in methanol-water and the pK and pH values of buffers. Anal. Chem 68 (1996) 3651-3657
19. Fink A.L., Calciano L.J., Goto Y., Kurotsu T., and Palleros D.R. Classification of acid denaturation of proteins. Intermediates and unfolded states. Biochemistry 33 (1994) 12504-12511
20. Mattice W.L., and Harrison W.H. Estimation of the Circular Dichroism Exhibited by Statistical Coils of Poly(L-Alanine) and Unionized Poly(L-Lysine) in Water. Biopolymers 14 (1975) 2025-2033
21. Buck M. Trifluoroethanol and colleagues. Cosolvents come of age. Recent studies with peptides and proteins. Q. Rev. Biophys 31 (1998) 297-355
22. Hirota-Nakaoka N., and Goto Y. Alcohol-induced denaturation of â-Lactoglobulin. A close correlation to the alcohol-induced α-helix formation of melittin. Bioorg. Med. Chem 7 (1999) 67-73
23. Bushnell G.W., Louie G.V., and Brayer G.D. High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol 214 (1990) 585
24. Konermann L., and Douglas D.J. Acid-induced unfolding of cytochrome c at different methanol concentrations. electrospray ionization mass spectrometry specifically monitors changes in tertiary structure. Biochemistry 36 (1997) 12296-12302
25. Suzumura A., Paul D., Sugimoto H., Shinoda S., Julian R.R., Beauchamp J.L., Teraoka J., and Tsukube H. Cytochrome c-crown ether complexes as supramolecular catalysts. Cold-active synzymes for asymmetric sulfoxide oxidation in methanol. Inorg. Chem 44 (2005) 904-910
26. Vijay-Kumar S., Bugg C.E., and Cook W.J. Structure of ubiquitin refined at 1.8 A resolution. J. Mol. Biol 194 (1987) 531-544
27. Brutscher B., Bruschweiler R., and Ernst R.R. Backbone dynamics and structural characterization of the partially folded A state of ubiquitin by 1H, 13C, and 15N nuclear magnetic resonance spectroscopy. Biochemistry 36 (1997) 13043-13053
28. Ecker D.J., Butt T.R., Marsh J., Sternberg E., Shatzman A., Dixon J.S., Weber P.L., and Crooke S.T. Ubiquitin functions studied by disulfide engineering. J. Biol. Chem 264 (1989) 1887-1893
29. Hoerner J.K., Xiao H., and Kaltashov I.A. Structural and dynamic characteristics of a partially folded state of ubiquitin revealed by hydrogen exchange mass spectrometry. Biochemistry 44 (2005) 11286-11294
30. Dill K.A., and Shortle D. Denatured states of proteins. Annu. Rev. Biochem 60 (1991) 795-825
31. 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) 4139-4147
32. Wang F., and Polavarapu P.L. Conformational analysis of melittin in solution phase. Vibrational circular dichroism study. Biopolymers 70 (2003) 614-619
33. Hirota N., Mizuno K., and Goto Y. Group additive contributions to the alcohol-induced α-helix formation of melittin. Implication for the mechanism of the alcohol effects on proteins. J. Mol. Biol 275 (1998) 365-378
34. Bazzo R., Tappin M.J., Pastore A., Harvey T.S., Carver J.A., and Campbell I.D. The structure of melittin. A 1H-NMR study in methanol. Eur. J. Biochem 173 (1988) 139-146
35. Eisenberg, D.; Gribskov, M.; Terwilliger, T. C. PDB ID: 2MLT; unpublished.