Hydrogen exchange demonstrates three domains in aldolase unfold sequentially

Journal of Molecular Biology

Volumn 294, Issue 1, 1999, Pages 247-258

  Deng, Yuzhong ^a   Smith, David L ^a  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

Author keywords

Aldolase; Hydrogen exchange; Mass spectrometry; Unfolding

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; HYDROGEN; UREA;

ARTICLE; CIRCULAR DICHROISM; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBUNIT; MASS SPECTROMETRY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; RABBIT;

ORYCTOLAGUS CUNICULUS;

EID: 0033585130     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3251     Document Type: Article

References (30)

1. Bai Y., Milne J. S., Mayne L., Englander S. W. Primary structure effects on peptide group hydrogen exchange. Proteins: Struct. Funct. Genet. 17:1993;75-86.
2. Bai Y., Sosnick T. R., Mayne L., Englander S. W. Protein folding intermediates: Native-state hydrogen exchange. Science. 269:1995;192-197.
3. Barshop B. A., Wrenn R. F., Frieden C. KIMSIM/FITSIM. Anal. Biochem. 130:1983;134-145.
4. Bilsel O., Zitzewitz J. A., Bowers K. E., Matthews C. R. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry. 38:1999;1018-1029.
5. Blom N., Sygusch J. Product binding and role of the C-terminal region in Class I D-fructose 1,6-bisphosphate aldolase. Nature Struct. Biol. 4:1997;36-39.
6. Bryngelson J. D., Wolynes P. G. A simple statistical field theory of heteropolymer collapse with application to protein folding. Biopolymers. 30:1990;177-188.
7. Chamberlain A. K., Handel T. M., Marqusee S. Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. Nature Struct. Biol. 3:1996;782-787.
8. Deng Y., Smith D. L. Identification of unfolding domains in large proteins by their unfolding rates. Biochemistry. 37:1998;6256-6262.
9. Deng Y., Pan H., Smith D. L. Selective isotope labeling demonstrates that hydrogen exchange at individual peptide amide linkages can be determined by collision-induced dissociation mass spectrometry. J. Am. Chem. Soc. 121:1999a;1966-1967.
10. Deng Y., Zhang Z., Smith D. L. Comparison of continuous and pulsed labeling amide hydrogen exchange/mass spectrometry for studies of protein dynamics. J. Am. Soc. Mass Spectrom. 10:1999b;675-684.
11. Eder J., Kirschner K. Stable substructures of eight-fold beta alpha-barrel proteins: fragment complementation of phosphoribosylanthranilate isomerase. Biochemistry. 31:1992;3617-3625.
12. Engen J. R., Smithgall T. E., Gmeiner W. H., Smith D. L. Identification and localization of slow, natural, cooperative unfolding in the hematopoietic cell kinase SH3 domain by amide hydrogen exchange and mass spectrometry. Biochemistry. 36:1997;14384-14391.
13. Englander J. J., Rogero J. R., Englander S. W. Protein hydrogen exchange studied by the fragment separation method. Anal. Biochem. 147:1985;234-244.
14. Fuentes E. J., Wand A. J. Local dynamics and stability of apocytochrome b562 examined by hydrogen exchange. Biochemistry. 37:1998;3687-3698.
15. Heidary D. K., Gross L. A., Roy M., Jennings P. A. Evidence for an obligatory intermediate in the folding of interleukin-1. beta. Nature Struct. Biol. 4:1997;725-731.
16. Hsu L.-S., Neet K. E. Subunit interactions of rabbit muscle aldolase. Dissociation of aldolase in 1.2 M magnesium chloride. Biochemistry. 12:1973;586-595.
17. Hvidt A., Nielsen S. O. Hydrogen exchange in proteins. Advan. Protein Chem. 21:1966;287-385.
18. Itzhaki L. S., Neira J. L., Fersht A. R. Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature. J. Mol. Biol. 270:1997;89-98.
19. Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
20. Miller D. W., Dill K. A. A statistical mechanical model for hydrogen exchange in globular proteins. Protein Sci. 4:1995;1860-1873.
21. Miranker A., Robinson C. V., Radford S. E., Aplin R. T., Dobson C. M. Detection of transient protein folding populations by mass spectrometry. Science. 262:1993;896-900.
22. Parker M. J., Spencer J., Clarke A. R. An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J. Mol. Biol. 253:1995;771-786.
23. Parker M. J., Dempsey C. E., Lorch M., Clarke A. R. Acquisition of native beta-strand topology during the rapid collapse phase of protein folding. Biochemistry. 36:1997;13396-13405.
24. Sanchez del Pino M. M., Fersht A. R. Nonsequential unfolding of the alpha/beta barrel protein indole-3-glycerol-phosphate synthase. Biochemistry. 36:1997;5560-5565.
25. Smith D. L., Deng Y., Zhang Z. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J. Mass Spectrom. 32:1997;135-146.
26. Thévenon-Emeric G., Kozlowski J., Zhang Z., Smith D. L. Determination of amide hydrogen exchange rates in peptides by mass spectrometry. Anal. Chem. 64:1992;2456-2458.
27. Xu Y., Mayne L., Englander S. W. Evidence for an unfolding and refolding pathway in cytochrome c. Nature Struct. Biol. 5:1998;774-778.
28. Yang H., Smith D. L. Kinetics of cytochrome c folding examined by hydrogen exchange and mass spectrometry. Biochemistry. 36:1997;14992-14999.
29. Yi Q., Baker D. Direct evidence for a two-state protein unfolding transition from hydrogen-deuterium exchange, mass spectrometry, and NMR. Protein Sci. 5:1996;1060-1066.
30. Zhang Z., Smith D. L. Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci. 2:1993;522-531.