An evaluation of the use of hydrogen exchange at equilibrium to probe intermediates on the protein folding pathway

Folding and Design

Volumn 1, Issue 4, 1996, Pages 243-254

  Clarke, Jane ^a   Fersht, Alan R ^a  

^a MEDICAL RESEARCH COUNCIL   (United Kingdom)

Author keywords

Barnase; Hydrogen deuterium exchange; NMR; Protein folding

Indexed keywords

AMIDE; BACILLUS AMYLOLIQUEFACIENS RIBONUCLEASE; DEUTERIUM; HYDROGEN; PROTEIN; PROTON; RIBONUCLEASE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; HYDROGEN BOND; PROTEIN DENATURATION; PROTEIN FOLDING; THERMODYNAMICS;

AMIDES; DEUTERIUM; HYDROGEN; HYDROGEN BONDING; MOLECULAR STRUCTURE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEINS; PROTONS; RIBONUCLEASES; THERMODYNAMICS;

EID: 0030334648     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00038-7     Document Type: Article

References (37)

1. Wagner, G. & Wütrich, K. (1982). Amide proton exchange and surface conformation of BPTI in solution. J. Mol. Biol. 160, 343-361.
2. Englander, S.W. & Kallenbach, N.R. (1984). Hydrogen exchange and structural dynamics of proteins and nucleic acids. Quart. Rev. Biophys. 16, 521-655.
3. Pedersen, T.G., et al., & Redfield, C. (1991). A NMR study of the hydrogen-exchange behaviour of lysozyme in crystals and solution. J. Mol. Biol. 218, 413-426.
4. Gallagher, W., Tao, F. & Woodward, C. (1992). Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution. Biochemistry 31, 4673-4680.
5. 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 14, 237-248.
6. Kim, K., Fuchs, J.A. & Woodward, C.K. (1993). Hydrogen exchange identifies native state motional domains important in protein folding. Biochemistry 32, 9600-9608.
7. Hvidt, A.A. & Neilsen, S.O. (1966). Hydrogen exchange in proteins. Adv. Protein Chem. 21, 287-386.
8. Woodward, C.K. & Hilton, B.D. (1979). Hydrogen exchange kinetics and internal motions in proteins and nucleic acids. Annu. Rev. Biophys. Bioeng. 8, 99-127.
9. 2H and temperature. Biochemistry 24, 7396-7407.
10. Jeng, M. & Englander, S.W. (1991). Stable submolecular folding units in a non-compact form of cytochrome c. J. Mol. Biol. 221, 1045-1061.
11. Linderstrøm-Lang, K. (1955). Deuterium exchange between peptides and water. Chem Soc. (London), Spec. Publ. 2, 1-20.
12. Mayo, S.L. & Baldwin, R.L (1993). Guanidinium chloride induction of partial unfolding in amide proton exchange in RNase A. Science 262, 873-876.
13. Bai, Y., Sosnick, T.R., Mayne, L. & Englander, S.W. (1995). Protein folding intermediates: native state hydrogen exchange. Science 269, 192-197.
14. Tanford, C. (1970). Protein folding. Part C. Adv. Protein Chem. 24, 1-95.
15. Bai, Y., Milne, J.S., Mayne, L. & Englander, W.S. (1994). Protein stability parameters measured by hydrogen exchange. Proteins 20, 4-14.
16. Clarke, J., Hounslow, A.M., Bycroft, M. & Fersht, A.R. (1993). Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways. Proc. Natl. Acad. Sci. USA 90, 9837-9841.
17. Perrett, S., Clarke, J., Hounslow, A.M. & Fersht, A.R. (1995). The relationship between equilibrium amide proton exchange behavior and the folding pathway of barnase. Biochemistry 34, 9288-9293.
18. Matouschek, A., Serrano, L. & Fersht, A.R. (1992). The folding of an enzyme IV. Structure of the intermediate in the refolding of barnase analysed by a protein engineering procedure. J. Mol. Biol. 224, 819-835.
19. Qian, H., Mayo, S.L. & Morton, A. (1994). Protein hydrogen exchange in denaturant: quantitative analysis by a two-process model. Biochemistry 33, 8167-8171.
20. Delepierre, M., Dobson, C.M., Selvarajah, S., Wedix, R.E. & Poulsen, F.M. (1983). Correlation of hydrogen exchange behaviour and thermal stability of lysozyme. J. Mol. Biol. 168, 687-692.
21. Roder, H., Wagner, G. & Wütrich, K. (1985). Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitor. Biochemistry 24, 7407-7411.
22. Kim, K.-S. & Woodward, C. (1993). Protein internal flexibility and global stability: effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry 32, 9609-9613.
23. Loh, S.N., Rohl, C.A., Kiefhaber, T. & Baldwin, R.L. (1996). A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions. Proc. Natl. Acad. Sci. USA 93, 1982-1987.
24. Bai, Y., Milne, J.S., Mayne, L. & Englander, S.W. (1993). Primary structure effects on peptide group hydrogen exchange. Proteins 17, 75-86.
25. Clarke, J. & Fersht, A.R. (1993). Engineering disulfide bonds as probes of the folding pathway of barnase: increasing the stability of proteins against the rate of denaturation. Biochemistry 32, 4322-4329.
26. Molday, R.S., Englander, S.W. & Kallen, R.G. (1972). Primary structure effects on peptide group hydrogen exchange. Biochemistry 11, 150-158.
27. Miranker, A., Robinson, C., Radford, S. & Dobson, C.M. (1993). Detection of transient protein folding populations by mass spectrometry. Science 262, 896-900.
28. Skelton, N.J., Kordel, J., Akke, M. & Chazin, W.J. (1992). Nuclear magnetic resonance studies of the internal dynamics in Apo, (Cd2+)1 and (Ca2+)2 calbindin D9k. The rates of amide proton exchange with solvent. J. Mol. Biol. 227, 1100-1117.
29. Connelly, G.P., Bai, Y., Jeng, M.-F. & Englander, S.W. (1993). Isotope effect in peptide group hydrogen exchange. Proteins 17, 87-92.
30. 1H NMR assignments of its pH-denatured state. Proc. Natl. Acad. Sci. USA 91, 9412-9416.
31. Miller, D.W. & Dill, K.A. (1995). A statistical mechanical model for hydrogen exchange in globular proteins. Protein Sci. 4, 1860-1873.
32. Meiering, E.M., Bycroft, M. & Fersht, A.R. (1991). Characterization of phosphate binding in the active site of barnase by site-directed mutagenesis and NMR. Biochemistry 30, 11348-11356.
33. Woodward, C. (1993). Is the slow-exchange core the protein folding core? Trends Biochem. Sci. 18, 359-360.
34. Woodward, C.K. (1994). Hydrogen exchange rates and protein folding. Curr. Opin. Struct. Biol. 4, 112-116.
35. Glasoe, P.F. & Long, F.A. (1960). Use of a glass electrode to measure acidities in deuterium oxide. J. Phys. Chem. 64, 188-193.
36. Bax, A., Ikura, M., Kay, LE., Torchia, D.A. & Tschudin, R. (1990). Comparison of different modes of 2-dimensional reverse correlation NMR for the study of proteins. J. Magn. Reson. 86, 304-318.
37. Mauguen, Y., et al., & Jack, A. (1982). Molecular structure of a new family of ribonucleases. Nature 297, 162-164.