Thermally induced hydrogen exchange processes in small proteins as seen by FTIR spectroscopy

Proteins: Structure, Function and Genetics

Volumn 24, Issue 3, 1996, Pages 379-387

  Backmann, Jan ^a   Schultz, Christian ^a   Fabian, Heinz ^b   Hahn, Ulrich ^d   Saenger, Wolfram ^c   Naumann, Dieter ^a  

^a ROBERT KOCH INSTITUTE   (Germany)

^b HUMBOLDT UNIVERSITY   (Germany)

^c FREIE UNIVERSITÄT BERLIN   (Germany)

^d UNIVERSITY OF LEIPZIG   (Germany)

Author keywords

histone like protein HBsu; infrared spectroscopy; protein structure; RNase A; RNase T1; unfolding

Indexed keywords

AMIDE; PROTEIN;

ARTICLE; ENERGY; HEATING; INFRARED SPECTROSCOPY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; THERMAL EXPOSURE;

AMIDES; DEUTERIUM; HYDROGEN; PROTEINS; PROTONS; RIBONUCLEASE, PANCREATIC; SOLUTIONS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

EID: 0029883792     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199603)24:3<379::AID-PROT11>3.0.CO;2-J     Document Type: Article

References (32)

1. Hvidt, A., Nielsen, S.O. Hydrogen exchange in proteins. Adv. Protein Chem. 21:287-386, 1966.
2. Englander, S.W., Kallenbach, N. Hydrogen exchange and structural dynamics of proteins and nucleic acids. Q. Rev. Biophys. 16:521-655, 1984.
3. Mayo, S.L., Baldwin, R.L. Guanidinium cloride induction of partial unfolding in amide proton exchange. Science 262:873-876, 1993.
4. Qian, H., Mayo, S L., Morton, A. Protein hydrogen exchange in denaturant: Quantitative analysis by two-process model. Biochemistry 33:8167-8171, 1994.
5. Englander, S W., Englander, J.J., McKinnie, R.E., Ackers, G.K., Turner, G.J., Westrick, J.A., Stanley J.G. Hydrogen exchange measurement of free energy of structural and allosteric change in hemoglobin. Science 256:1684-1686, 1992.
6. Clarke, J., Hounslow, A.M., Bycroft, M., Fersht, A.R. Local breathing and global unfolding in hydrogen exchange of barnase and its relationship to protein folding pathways. Proc. Natl. Acad. Sci. U.S.A. 90:9837-9841, 1993.
7. Bai, Y., Milne, J.S., Mayne, L., Englander, S.W. Protein stability parameters measured by hydrogen exchange. Proteins 20:4-14, 1994.
8. Kossiakoff, A.A. Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique. Nature 296:713-721, 1982.
9. Jacobs, M.J., Fox, R.O. Staphylococcal nuclease folding intermediate characterized by hydrogen exchange and NMR spectroscopy. Proc. Natl. Acad. Sci. U.S.A. 91:449-453, 1994.
10. Wlodawer, A., Sjölin, L. Hydrogen exchange in RNase A: Neutron diffraction study. Proc. Natl. Acad. Sci. U.S.A. 79:1418-1422, 1982.
11. -1 in Proteins. Nature 172:770-771, 1953.
12. Blout, E.R., de Loze, C., Asadourian, A. The deuterium exchange of water-soluble polypeptides and proteins as measured by infrared spectroscopy. J. Am. Chem. Soc. 83: 1895-1900, 1961.
13. Nakanishi, M., Tsuboi, M., Ikegami, A. Fluctuation of lysozyme structure J. Mol. Biol. 70:351-361, 1972.
14. Nakanishi, M., Tsuboi, M., Ikegami, A. Fluctuation of lysozyme structure J. Mol. Biol. 75:673-682, 1973.
15. Nakanishi, M., Tsuboi, M., Ikegami, A. Fluctuation of the myoglobin structure. Bull. Chem. Soc. Japan 47:293-298, 1974.
16. Nakanishi, M., Tsuboi, M. Determination of the number of hydrogen-bonds in a protein molecule. Bull. Chem. Soc. Japan 47:305-307, 1974.
17. Hvidt, A., Pedersen, E.J. A comparative study on the basic trypsin inhibitor and insulin by the hydrogen-exchange method. Eur. J. Biochem. 48:333-338, 1974.
18. Pershina, L., Hvidt, A. A study by hydrogen-exchange method of complex formed between the basic pancreatic trypsin inhibitor and trypsin. Eur. J. Biochem. 48:339-344, 1974.
19. Segawa, S.-I., Kume, K. Lysozyme-effects of denaturants, ligand binding and interchain cross-linking on hydrogen exchange and unfolding kinetics. Biopolymers 25:1981-1996, 1986.
20. 2O solutions. Biochim. Biophys. Acta 869:89-98, 1986.
21. Wantyghem, J., Baron, M.-H., Picquart, M., Lavialle, F. Conformational changes of Robinia pseudoacacia lectin related to modifications of environment: FTIR investigation. Biochemistry 1990:6600-6609, 1990.
22. de Jongh, H.H.J., Goormaghtigh, E., Ruyshasshaert, J.-M. Tertiary stability of native and methionine-80 modified cytochrome c detected by proton-deuterium exchange using on-line Fourier transform infrared spectroscopy. Biochemistry 34:172-179, 1995.
23. Fabian, H., Schultz, C., Neumann, D., Landt, O., Hahn, U., Saenger, W. Secondary structure and temperature-induced unfolding and refolding of ribonuclease T1 in aqueous solution. J. Mol. Biol 232:967-981, 1993.
24. Fabian, H., Schultz, C., Backmann, J., Hahn, U., Saenger, W., Mantsch, H.H., Naumann, D. Impact of point mutations on the structure and thermal stability of ribonuclease T1 in aqueuos solution probed by Fourier transform infrared spectroscopy. Biochemistry 33:10725-10730, 1994.
25. Quass, R., McKeown, Y., Stansens, P., Frank, R., Blöcker, H., Hahn, U. Expression of chemically synthesized gene of ribonuclease T1 in Escherichia coli using a secretion cloning vector. Eur. J. Biochem. 173:617-622, 1988.
26. Landt, O., Zirpel-Giesbrecht, M., Milde, A., Hahn, U. Improving purification of recombinant ribonuclease T1 J. Biotechnol. 24:189-194, 1992.
27. Kaupinnen, J.K., Moffat, D J., Mantsch, H.H., Cameron, D.G. Fourier self-deconvolution: A method for resolving intrinsically overlapping bands. Appl. Spectrosc. 35:271-276, 1981.
28. Backmann, J., Fabian, H., Naumann, D. Temperature-jump induced refolding of ribonuclease A: A time-resolved FTIR spectroscopic study. FEBS Lett. 364:175-178, 1995.
29. Pace, C.N., Grimsley, G R., Thomson, J.A., Barnett, B.J. Conformational stbility and activity of ribonuclease T1 with zero, one, and two intact disulfide bonds. J. Biol. Chem. 263:11820-11825, 1988.
30. Tanaka, I., Appelt, K., Dijk, J., White, S.W., Wilson, K.S. 3-Å resolution structure of a protein with histone-like properties in prokariotes. Nature 310:376-381, 1984.
31. Wagner, G., Wütherich, K. Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor. J. Mol. Biol. 130:31-37, 1979.
32. Schubert, W.-D., Schluckebier, G., Backmann, J., Granzin, J., Kisker, C., Choe, H.-W., Hahn, U., Pfeil, W., Saenger, W. X-ray crystallographic and calorimetric studies of effects of the mutation Trp59→Tyr in ribonuclaese T1. Eur. J. Biochem. 220:527-534, 1994.