Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions

Journal of Molecular Biology

Volumn 334, Issue 2, 2003, Pages 293-307

  Nishimura, Chiaki ^a   Wright, Peter E ^a   Dyson, H Jane ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

Mass spectrometry; Mutant; Myoglobin; NMR; Quench flow hydrogen exchange

Indexed keywords

APOMYOGLOBIN; HYDROGEN; MYOGLOBIN; PROTEIN; PROTON;

AMINO ACID SUBSTITUTION; ARTICLE; COMPARATIVE STUDY; DATA ANALYSIS; DNA HELIX; EVIDENCE BASED MEDICINE; FLUORESCENCE; ION EXCHANGE; KINETICS; MASS SPECTROMETRY; MUTANT; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; WILD TYPE;

EID: 0242321015     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.042     Document Type: Article

References (24)

1. Jennings P.A., Wright P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science. 262:1993;892-896.
2. Nishimura C., Dyson H.J., Wright P.E. The apomyoglobin folding pathway revisited: structural heterogeneity in the kinetic burst phase intermediate. J. Mol. Biol. 322:2002;483-489.
3. Tsui V., Garcia C., Cavagnero S., Siuzdak G., Dyson H.J., Wright P.E. Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through an obligatory intermediate. Protein Sci. 8:1999;45-49.
4. Jamin M., Baldwin R.L. Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin. Nature Struct. Biol. 3:1996;613-618.
5. Jamin M., Baldwin R.L. Two forms of the pH 4 folding intermediate of apomyoglobin. J. Mol. Biol. 276:1998;491-504.
6. Eliezer D., Chung J., Dyson H.J., Wright P.E. Native and non-native structure and dynamics in the pH 4 intermediate of apomyoglobin. Biochemistry. 39:2000;2894-2901.
7. Eliezer D., Yao J., Dyson H.J., Wright P.E. Structural and dynamic characterization of partially folded states of myoglobin and implications for protein folding. Nature Struct. Biol. 5:1998;148-155.
8. Griko Y.V., Privalov P.L., Venyaminov S.Y., Kutyshenko V.P. Thermodynamic study of the apomyoglobin structure. J. Mol. Biol. 202:1988;127-138.
9. Hughson F.M., Baldwin R.L. Use of site-directed mutagenesis to destabilize native apomyoglobin relative to folding intermediates. Biochemistry. 28:1989;4415-4422.
10. Feng Z.Y., Ha J.H., Loh S.N. Identifying the site of initial tertiary structure disruption during apomyoglobin unfolding. Biochemistry. 38:1999;14433-14439.
11. Garcia C., Nishimura C., Cavagnero S., Dyson H.J., Wright P.E. Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue. Biochemistry. 39:2000;11227-11237.
12. Udgaonkar J.B., Baldwin R.L. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Nature. 335:1988;694-699.
13. Roder H., Elöve G.A., Englander S.W. Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature. 335:1988;700-704.
14. 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.
15. 1H NMR spectra. Protein Sci. 9:2000;186-193.
16. Jennings P.A., Stone M.J., Wright P.E. Overexpression of myoglobin and assignment of the amide, Cα and Cβ resonances. J. Biomol. NMR. 6:1995;271-276.
17. Padmanabhan S., Marqusee S., Ridgeway T., Laue T.M., Baldwin R.L. Relative helix-forming tendencies of nonpolar amino acids. Nature. 344:1990;268-270.
18. Kuriyan J., Wilz S., Karplus M., Petsko G.A. X-ray structure and refinement of carbon-monoxy (Fe II)-myoglobin at 1.5 Å resolution. J. Mol. Biol. 192:1986;133-154.
19. Grzesiek S., Bax A. An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J. Magn. Reson. 99:1992;201-207.
20. Wittekind M., Mueller L. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J. Magn. Reson. 101:1993;201-205.
21. Grzesiek S., Bax A. Correlating backbone amide and side-chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chem. Soc. 114:1992;6291-6293.
22. Marion D., Ikura M., Tschudin R., Bax A. Rapid recording of 2D NMR spectra without phase cycling. Application to the study of hydrogen exchange in proteins. J. Magn. Reson. 85:1989;393-399.
23. Delaglio F., Grzesiek S., Vuister G.W., Guang Z., Pfeifer J., Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6:1995;277-293.
24. Johnson B.A., Blevins R.A. NMRView: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR. 4:1994;604-613.