Enhanced correction methods for hydrogen exchange-mass spectrometric studies of amyloid fibrils

Protein Science

Volumn 12, Issue 3, 2003, Pages 635-643

  Kheterpal, Indu ^a   Wetzel, Ronald ^a   Cook, Kelsey D ^b  

^a UNIVERSITY OF TENNESSEE MEDICAL CENTER   (United States)

^b UNIVERSITY OF TENNESSEE   (United States)

Author keywords

A amyloid; Electrospray ionization; Hydrogen exchange; Mass spectrometry

Indexed keywords

AMIDE; AMYLOID; DEUTERIUM; HYDROGEN;

ALGORITHM; ARTICLE; MASS SPECTROMETRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; QUANTITATIVE ANALYSIS;

AMYLOID BETA-PROTEIN; HUMANS; HYDROGEN; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 0037372212     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0225703     Document Type: Article

References (34)

1. Anderson, M.D., Shaffer, J., Jennings, P.A., and Adams, J.A. 2001. Structural characterization of protein kinase A as a function of nucleotide binding. J. Biol. Chem. 17: 14204-14211.
2. Buxbaum, J.N. and Tagoe, C.E. 2000. The genetics of the amyloidoses. Annu. Rev. Med. 51: 543-569.
3. Dempsey, C.E. 2001. Hydrogen exchange in peptides and proteins using NMR spectroscopy. Progress in Nuclear Magnetic Resonance Spectroscopy 39: 135-170.
4. Egnaczyk, G.F., Greis, K.D., Stimson, E.R., and Maggio, J.E. 2001. Photoaffinity cross-linking of Alzheimer's disease amyloid fibrils reveals inter-strand contact regions between assembled β-amyloid peptide subunits. Biochemistry 40: 11706-11714.
5. Ehring, H. 1999. Hydrogen exchange/electrospray ionization mass spectrometry studies of structural features of proteins and protein/protein interactions. Anal. Biochem. 267: 252-259.
6. Engen, J.R., Bradbury, E.M., and Chen, X. 2002. Using stable-isotope-labeled proteins for hydrogen exchange studies in complex mixtures. Anal. Chem. 74: 1680-1686.
7. Englander, S.W. and Kallenbach, N.R. 1983. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16: 521-655.
8. Harris, D.C. 1998. Quantitative chemical analysis, 5th ed. W.H. Freeman, New York.
9. Hernandez, H. and Robinson, C.V. 2001. Dynamic protein complexes: Insights from mass spectrometry. J. Biol. Chem. 276: 46685-46688.
10. 2-microglobulin amyloid fibril by H/D exchange. Nat. Struct. Biol. 9: 332-336.
11. Ippel, J.H., Olofsson, A., Schleucher, J., Lundgren, E., and Wijmenga, S.S. 2002. Probing solvent accessibility of amyloid fibrils by solution NMR spectroscopy. Proc. Natl. Acad. Sci. 99: 8648-8653.
12. Johnson, R.S. and Walsh, K.A. 1994. Mass spectrometric measurement of protein amide hydrogen exchange rates of apo- and holo-myoglobin. Protein Sci. 3: 2411-2418.
13. Katta, V. and Chait, B.T. 1991. Conformational changes in proteins probed by hydrogen-exchange electrospray-ionization mass spectrometry. Rapid Commun. Mass Spectrom. 5: 214-217.
14. Kheterpal, I., Zhou, S., Cook, K.D., and Wetzel, R. 2000. Aβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange. Proc. Natl. Acad. Sci. 97: 13597-13601.
15. Kheterpal, I., Williams, A., Murphy, C., Bledsoe, B., and Wetzel, R. 2001. Structural features of the Aβ amyloid fibril elucidated by limited proteolysis. Biochemistry 40: 11757-11767.
16. Li, R. and Woodward, C. 1999. The hydrogen exchange core and protein folding. Protein. Sci. 8: 1571-1591.
17. Mandell, J.G., Falick, A.M., and Komives, E.A. 1998. Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry. Anal. Chem. 70: 3987-3995.
18. Prusiner, S.B. 2001. Shattuck lecture - Neurodegenerative diseases and prions. N. Engl. J. Med. 344: 1516-1526.
19. Resing, K.A., Hoofnagle, A.N., and Ahn, N.G. 1999. Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure. J. Am. Soc. Mass Spectrom. 10: 685-702.
20. Selkoe, D.J. 1994. Normal and abnormal biology of the β-amyloid precursor protein. Annu. Rev. Neurosci. 17: 489-517.
21. Serpell, L.C. 2000. Alzheimer's amyloid fibrils: Structure and assembly. Biochim Biophys Acta 1502: 16-30.
22. Serpell, L.C., Blake, C.C., and Fraser, P.E. 2000. Molecular structure of a fibrillar Alzheimer's Aβ fragment. Biochemistry 39: 13269-13275.
23. Sipe, J.D. and Cohen, A.S. 2000. Review: History of the amyloid fibril. J. Struct. Biol. 130: 88-98.
24. Smith, D.L., Deng, Y., and Zhang, Z. 1997. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J. Mass Spectrom. 32: 135-146.
25. Tito, P., Nettleton, E.J., and Robinson, C.V. 2000. Dissecting the hydrogen exchange properties of insulin under amyloid fibril forming conditions: A site-specific investigation by mass spectrometry. J. Mol. Biol. 303: 267-278.
26. Tobler, S.A. and Fernandez, E.J. 2002. Structural features of interferon-γ aggregation revealed by hydrogen exchange. Protein. Sci. 11: 1340-1352.
27. Tycko, R. 2000. Solid-state NMR as a probe of amyloid fibril structure. Curr. Opin. Chem. Biol. 4: 500-506.
28. Wang, F., Scapin, G., Blanchard, J.S., and Angeletti, R.H. 1998. Substrate binding and conformational changes of Clostridium glutamicium diaminopimelate dehydrogenase revealed by hydrogen/deuterium exchange and electrospray mass spectrometry. Protein Sci. 7: 293-299.
29. 2+ induced conformational changes in the regulatory domain of human cardiac troponin C. J. Am. Soc. Mass Spectrom. 10: 703-710.
30. Westermark, P., Benson, M.D., Buxbaum, J.N., Cohen, A.S., Frangione, B., Ikeda, S., Masters, C.L., Merlini, G., Saraiva, M.J., and Sipe, J.D. 2002. Amyloid fibril protein nomenclature - 2002. Amyloid 9: 197-200.
31. Wuthrich, K. and Wagner, G. 1979. Nuclear magnetic resonance of labile protons in the basic pancreatic trypsin inhibitor. J. Mol. Biol. 130: 1-18.
32. Zagorski, M.G., Yang, J., Shao, H., Ma, K., Zeng, H., and Hong, A. 1999. Methodological and chemical factors affecting amyloid β peptide amyloidogenicity. Methods Enzymol. 309: 189-204.
33. Zhang, Y.H., Yan, X., Maier, C.S., Schimerlik, M.I., and Deinzer, M.L. 2001. Structural comparison of recombinant human macrophage colony stimulating factor β and a partially reduced derivative using hydrogen deuterium exchange and electrospray ionization mass spectrometry. Protein Sci. 10: 2336-2345.
34. 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.