Investigation of protein folding by mass spectrometry

FASEB Journal

Volumn 10, Issue 1, 1996, Pages 93-101

  Miranker, Andrew ^a   Robinson, Carol V ^a   Radford, Sheena E ^a,b   Dobson, Christopher M ^a,c  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF LEEDS   (United Kingdom)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

hydrogen exchange; molecular chaperone folding intermediate; oxidative refolding; peptide models

Indexed keywords

CHAPERONE; CHAPERONIN; LIGAND; PROTEIN;

CONFORMATIONAL TRANSITION; LIGAND BINDING; MASS SPECTROMETRY; MOLECULAR DYNAMICS; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT; REVIEW;

EID: 0030027339     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.10.1.8566553     Document Type: Review

References (47)

1. Dobson, C. M., ed (1995) Folding and binding. Curr. Opin. Struct. Blol. 5, 56-121
2. Miranker, A., Robinson, C. V., Radford, S. E., Aplin, R. T., and Dobson, C. M. (1993) Detection of transient protein folding populations by mass spectrometry. Science 262, 896-899
3. Zhang, Z., and Smith, D. L. (1993) Determination of amide hydrogen-exchange by mass-spectrometry: A new tool for protein structure elucidation. Protein Sci. 2, 522-531
4. Mann, M., and Wilm, M. (1995) Electrospray mass spectrometry for protein characterization. Trends Biochem. Sci. 20, 219-224
5. Feng, R., and Konishi, Y. (1993) Collisionally-activated dissociation of multiply charged 150-kDa antibody ions. Anal. Chem. 65, 645-649
6. Chen, R. D., Cheng, X H., Mitchell, D. W., Hofstadler, S. A., Wu, Q. Y., Rockwood, A. L., Sherman, M. G., and Smith, R. D. (1995) Trapping, detection, and mass determination of coliphage T4 DNA ions of 10(8) Da by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 67, 1159-1163
7. Smith, R. D., Cheng, X., Bruce, J. E., Hofstadler, S. A., and Anderson, G. A. (1994) Tiapping, detection and reaction of very large single molecular-ions by mass spectrometry. Nature (London) 369, 137-139
8. Andren, P. E., Emmett, M. R., and Caprioli, R. M. (1994) Micro-electrospray: zeptomole-attomole per microliter sensitivity for peptides. J. Am. Soc. Mass Spect. 5, 867-869
9. Hooke, S. D., Eyles, S. J., Miranker, A., Radford, S. E., Robinson, C. V., and Dobson, C. M. (1994) Cooperative elements in protein folding monitored by electrospray mass spectrometry. J. Am. Chem. Soc. 117, 7548-7549
10. Senko, M. W., and McLafferly, F. W. (1994) Mass spectrometry of macromolecules: Has its time now come? Annu. Rev. Biophys. Biomol. Struct. 23, 763-785
11. Torella, C., Ruoppolo, M., Marino, G., and Pucci, P. (1994) Analysis of RNase-A refolding intermediates by electrospray mass-spectrometry. FEBS Lett. 352, 301-306
12. Chowdhury, S. K., Katta, V., and Chait, B. T. (1990) Probing conformational-changes in proteins by mass spectrometry. J. Am. Chem. Soc. 112, 9012-9013
13. Mirza, U. A., Cohen, S. L., and Chait, B. T. (1993) Heat induced conformational changes in proteins studied by electrospray ionization mass spectrometry. Anal. Chem. 65, 1-6
14. Chan, C., Willis, A. C., Robinson, C. V., Aplin, R. T., Radford, S. E., and Ferguson, S. J. (1995) The complete amino acid sequence confirms the presence of pseudoazurin in Thiosphaera pantotropha. Biochem. J. 308, 585-590
15. Schnier, P. D., Gross. D. S., and Williams, E. R. (1995) Electrostatic forces and dielectric polarizability of multiply protonated gas phase cytochrome c ions probed by ion/molecule chemistry. J. Am. Chem. Soc. 117, 6747-6757
16. Muir, T. W., Williams, M. J., and Kent, S. B. H. (1995) Detection of synthetic protein isomers and conformers by electrospray mass spectrometry. Anal. Biochem. 224, 100-109
17. Freedman,R. B. (1995) The formation of protein disulfide bonds. Curr. Opin. Struct. Biol. 5, 85-91
18. Glocker, O., Arbogast, B., Milley, R., Cowgill, C., and Deinzer, M. L. (1994) Disulfide linkages in the in vitro refolded intermediates of recombinant human macrophage-colony-stimulating factor: Analysis of the sulfhydryl alkylation of free cysteine residues by fast atom bombardment mass spectromelry. Proc. Natl Acad. Sci. USA 91, 5868-5872
19. Creighton, T. E., and Ewbank, J. J. (1994) Disulfide-rearranged molten globule state of α-lactalbumin. Biochemistry 33, 1534-1538
20. Peng, Z. Y., Wu, L. C., Schulman, B. A., and Kim, P. S. (1995) Does the molten globule have a native-like tertiary fold? Philos. Trans. R. Soc. London Ser. B Biol. Sci. 348, 43-47
21. Morris, H. R., Pucci, P., Panico, M., and Marino, G. (1990) Protein folding refolding analysis by mass-spectrometry: Scrambling of disulfide bridges in insulin. Biochem. J. 268, 803-806
22. Katta, V., and Chait, B. T. (1991) Conformational changes in proteins probed by hydrogen exchange and electrospray mass spectrometry. Rapid Commun. Mass Spectrom. 5, 214-217
23. Hvidt, A., and Nielsen, S. O. (1966) Hydrogen exchange in proteins. Adv. Protein Chem. 21, 287-386
24. Bai, Y. W., Milne. J. S., Mayne, L., and Englander, S. W. (1993) Primary structure effects on peptide group hydrogen exchange. Proteins: Struct. Funct. Genet. 17, 75-86
25. Segawa, S. I., Nakayama, M., and Sakane, M. (1981) Rates of structural fluctuations of lysozyme in the range of thermal unfolding transition. Biopolymers 20, 1691-1705
26. Delepierre. M., Dobson, C.M., Karplus, M., Poulsen, F. M., States, D. J., and Wedin, R. E. (1987) Electrostatic effects and hydrogen exchange behavior in proteins: The pH-dependence of exchange-rates in lysozyms me. J. Mol. Biol. 197, 111-122
27. Radford, S. E., Buck, M., Topping. K. D., Dobson, C. M., Evans, P. A. (1992) Hydrogen exchange in native and denatured states of hen egg white lysozyme. Proteins: Struct. Funct. Genet. 14, 237-248
28. Dyson, H. J., and Wright, P. E. (1993) Peptide conformation and protein folding. Curr. Opin. Struct. Biol. 3, 60-65
29. Wagner, D. S., Melton, L. G., Yan, Y. B., Erickson, B. W., and Anderegg, R. J. (1994) Deuterium exchange of α-helices and β-sheets as monitored by electrospray ionization mass spectrometry. Protein Sci. 3, 1305-1314
30. Baldwin, R. L. (1993) Pulsed H/D-exchange studies of folding intermediates. Curr. Opin. Struct. Biol. 3, 84-91
31. Miranker, A., Radford, S. E., Karplus, M., and Dobson, C. M. (1991) Demonstration by NMR of folding domains in lysozyme, Nature (London) 349, 633-636
32. Radford, S. E., Dobson, C. M., and Evans, P A. (1992) The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature (London) 358, 302-307
33. Fersht, A. R. (1995) Characteiizing transition states in protein folding: An essential step in the puzzle. Curr. Opin. Struct. Biol. 5, 79-84
34. Eyles, S. J., Radford, S. E., Robinson, C. V., and Dobson, C. M. (1994) Kinetic consequences of the removal of a disulfide bond from hen egg white lysozyme. Biochemistry 33, 13038-13048
35. Serrano, L. (1994) Protein engineering and the dissection of protein folding pathways. Curr. Opin. Struct. Biol. 4, 107-111
36. Ellis, J. (1996) Protein folding in the cell: competing models of chaperonin function. FASEB J. 10, 20-26
37. Robinson, C. V., Gross, M., Eyles, S. J., Ewbank, J. J., Mayhew, M., Hartl, F. U., Dobson, C. M., and Radford, S. E. (1994) Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry. Nature (London) 372, 646-651
38. Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular protein structure. Proteins: Struct. Funct. Genet. 6, 87-103
39. Johnson, R. S., and Walsh, K. A. (1994) Mass spertrometric measurement of protein amide hydrogen exchange rates of apo- and holo-myoglobin. Protein Sci. 3, 2411-2418
40. Siuzdak, G. (1994) The emergence of mass spectrometry in biochemical research. Proc. Natl. Acad. Sci. USA 91, 11290-11297
41. Smith, R. D., and Light-Wahl, K. J. (1993) The observation of non-covalent interactions in solution by electrospray ionisation mass spectrometry: Promises, pitfalls and prognosis. Biol. Mass Spectrom. 22, 493-501
42. Anderegg. R. J., and Wagner, D. S. (1995) Mass spectrometric characterisation of a protein ligand interaction. J. Am. Chem. Soc. 117, 1374-1377
43. Kragelund, B. B., Robinson, C. V., Knudsen, J., Dobson, C. M., and Poulsen, F. M. (1995) Folding of a foui helix, bundle: Studies of Acyl-CoA binding protein, Biochemistry 34, 7217-7224
44. Wood, T. D., Chorush, R. A., Wampler, F. M., Little, D. P., Oconnoi. P. B., and MeLafferty, F. W. (1995) Gas phase folding and unfolding of cytochrome c cations. Proc. Natl. Acad. Sci. USA 92, 2451-2454
45. Wolynes, P. G. (1995) Biomolecular folding in vacuo!!!(?). Proc. Natl. Acad. Sci. USA 92, 2426-2427
46. Levinthal, C. (1968) Are there pathways for protein folding? J. Chem. Phys 65, 44-15
47. Privalov, P. L., and Gill, S. J. (1988) Stability of protein structure and hydrophobie interaction. Adv. Protein. Chem. 39, 191-234