Measurement of water-amide proton exchange rates in the denatured state of staphylococcal nuclease by a magnetization transfer technique

Proteins: Structure, Function and Genetics

Volumn 28, Issue 3, 1997, Pages 325-332

  Mori, Susumu ^a   Van Zijl, Peter C M ^a   Shortle, David ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Denatured state; Hydrogen exchange; Magnetization transfer; NMR; Staphylococcal nuclease

Indexed keywords

BACTERIAL PROTEIN; NUCLEASE;

ARTICLE; ENZYME DENATURATION; MATHEMATICAL ANALYSIS; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTON TRANSPORT; STAPHYLOCOCCUS; TRANSPORT KINETICS;

AMIDES; AMINO ACID SEQUENCE; MAGNETIC RESONANCE SPECTROSCOPY; MICROCOCCAL NUCLEASE; MODELS, MOLECULAR; PROTEIN DENATURATION; PROTONS; WATER;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS;

EID: 0030961391     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199707)28:3<325::AID-PROT3>3.0.CO;2-B     Document Type: Article

References (31)

1. Dill K.A., Shortle D. Denatured state of proteins. Annu. Rev. Biochem. 60:795-825, 1991
2. Shortle D. Denatured state of proteins and their roles in folding and stability. Curr. Opin. Struct. Biol. 3:66-74, 1993.
3. Dobson C.M. Unfolded proteins, compact states, and molten globules. Curr. Opin. Struct. Biol. 2:6-12, 1992.
4. Wuthrich K. NMR Assignments as a basis for structural characterization of denatured states of globular proteins. Curr. Opin. Struct. Biol. 4:93-99, 1994.
5. Shortle D. Structral analysis of non-native states of proteins by NMR methods. Curr. Opin. Struct. Biol. 6:24-30, 1996.
6. Wedin R.E. Mechanisms of hydrogen exchange in proteins from nuclear magnetic resonance studies of individual tryptophan indole NH hydrogens in lysozyme. Biochemistry 21:1098-1103, 1982.
7. Roder H., Wagner G., Wüthrich K. Individual amide proton exchange rates in thermally unfolded basic pancreatic trypsin inhibitors. Biochemistry 27:7407-7411, 1985.
8. Roder H. Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol. 176:446-473, 1989.
9. Jeng M.-F., Englander W., Elöve G.A., Wand A.J., Roder H. Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR. Biochemistry 29:10433-10437, 1990.
10. Hughson F.M., Wright P.E., Baldwin R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science 249:1544-1548, 1990.
11. Jeng M.-F., Englander S.W. Stable submolecular folding units in a non-compact form of cytochrome c. J. Mol. Biol. 221:1045-1061, 1991.
12. Robertson A., Baldwin R. Hydrogen exchange in thermally denatured ribonuclease A. Biochemistry 30:9907-9914, 1991.
13. Radford S.E., Buck M., Topping K.D., Dobson C.M., Evans P.A. Hydrogen exchange in native and denatured states of hen egg-white lysozyme. Proteins 14:237-248, 1992.
14. Buck M., Radford S.E., Dobson C.M. Amide hydrogen exchange in a highly denatured state: Hen egg-white lysozyme in urea. J. Mol. Biol. 237:247-254, 1994.
15. Spera S., Ikura M., Bax A. Measurement of the exchange rates of rapidly exchanging amide protons: Application to the study of calmodulin and its complex with a myosin light chain kinase fragment. J. Biomol. NMR 1:155-165, 1991.
16. Gemmecker G., Hahnke W., Kessler H. Measurement of fast proton exchange rates in isotropically labeled compounds. J. Am. Chem. Soc. 115:11620-11621, 1993.
17. Grzesiek S., Bax A. Measurement of amide proton exchange rates and NOEs with water in 13C/15N-enriched calcineurin B. J. Biomol. NMR 3:627-638, 1993.
18. Koide S., Jahnke W., Wright P.E. Measurement of intrinsic exchange rates of amide protons in a 15N-labeled peptide. J. Biomol. NMR 6:306-312, 1995.
19. Mori S., Johnson M.O., Berg J.M., van Zijl P.C.M. Water exchange filter (WEX filter) for nuclear magnetic resonance studies of macromolecules. J. Am. Chem. Soc. 116: 11982-11984, 1994.
20. Mori S., Abeygunawardana C., van Zijl P.C.M., Berg J. Water exchange filter with improved sensitivity (WEX II) to study solvent-exchangeable protons: Application to the consensus zinc finger peptide CP-1. J. Magn. Reson. B 110:96-101, 1996.
21. Mori S., Berg J.M., van Zijl P.C.M. Separation of intramolecular NOE and exchange peaks in water exchange spectroscopy using spin echo filters. J. Biomol. NMR 7:78-82, 1996.
22. Alexandrescu A.T., Abeygunawardana C., Shortle D. Structure and dynamics of a denatured 131-residue fragment of staphylococcal nuclease: A heteronuclear NMR study. Biochemistry 33:1063-1072, 1994.
23. Wang Y., Shortle D. The equilibrium folding pathway of staphylococcal nuclease: Identification of the most stable chain-chain interactions. Biochemistry 34:15895-15905, 1995.
24. Alexandrescu A., Shortle D. Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease. J. Mol. Biol. 242:527-546, 1994.
25. Wang Y., Shortle D. Dynamic bundle of four adjacent Hydrophobic segments in the denatured state of staphylococcal nuclease. Prot. Sci. 5:1898-1906, 1996.
26. Jeener J., Meier B.H., Bachmann P., Ernst R.R. Investigation of exchange process by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:4564-4553, 1979.
27. Schwartz A.L., Cutnell J.D. One-and two-dimensional NMR studies of exchanging amide protons in gluthathione. J. Magn. Reson. 53:398-411, 1983.
28. Mori S., Abeygunawardana C., Johnson M.O., Berg J., van Zijl P.C.M. Improved sensitivity of HSQC spectra of exchanging protons at short interscan delays using a new fast HSQC (FHSQC) detection scheme that avoids water saturation. J. Magn. Reson. 108:94-98, 1995.
29. Bai Y., Milne J.S., Mayne L., Englander S.W. Primary structure effects on peptide group hydrogen exchange. Proteins 17:75-86, 1993.
30. Mori S., Abey G., Berg J.M., van Zijl P.C.M. NMR study of rapidly exchanging backbone amide protons in staphylococcal nuclease and the correlation with structural and dynamic properties. J. Am. Chem. Soc. (in press).
31. Hynes T.R., Fox R.O. The crystal structure of staphylococcal nuclease refined at 1.7Å resolution. Proteins 10:92-105, 1991.