Cooperativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations

Nature Structural Biology

Volumn 4, Issue 11, 1997, Pages 925-930

  Luo, Yongzhang ^a   Kay, Michael S ^a   Baldwin, Robert L ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LACTALBUMIN; GLYCINE; MYOGLOBIN; PROLINE;

AMINO ACID SUBSTITUTION; ARTICLE; CIRCULAR DICHROISM; ESCHERICHIA COLI; FAST PROTEIN LIQUID CHROMATOGRAPHY; GENE MUTATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; WHALE;

ANIMALS; APOPROTEINS; CIRCULAR DICHROISM; GLYCINE; HYDROGEN-ION CONCENTRATION; MUTATION; MYOGLOBIN; PROLINE; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE; WHALES;

CETACEA; ESCHERICHIA COLI;

EID: 0030694241     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb1197-925     Document Type: Article

References (24)

1. Takano, T. Structure of myoglobin refined at 2.0 Å resolution I. crystallographic refinement of metmyoglobin from sperm whale. J. Mol. Biol. 110, 537-568 (1977).
2. Kay, M.S. & Baldwin, R.L. Packing interactions in the apomyoglobin folding intermediate. Nature Struct. Biol. 3, 439-445 (1996).
3. Jamin, M. & Baldwin, R.L. Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin. Nature Struct. Biol. 3, 613-618 (1996).
4. Schulman, B.A. & Kim, P.S. Proline scanning mutagenesis of a molten globule reveals noncooperative formation of a protein's overall topology. Nature Struct. Biol. 3, 682-687 (1996).
5. Hughson, F.M., Wright, P.E., & Baldwin, R.L. Structural characterization of a partly folded apomyoglobin intermediate. Science 249, 1544-1548 (1990).
6. Wong, K.P. & Tanford, C. Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions. J. Biol. Chem. 248, 8518-8523 (1973).
7. Kuwajima, K., Nitta, K., Yoneyama, M. & Sugai, S. Three-state denaturation of α-lactalbumin by guanidine hydrochloride. J. Mol. Biol. 106, 359-373 (1976).
8. Jennings, P.A. & Wright, P.E. Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 262, 892-896 (1993).
9. Loh, S.N., Kay, M.S. & Baldwin, R.L. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway. Proc. Natl. Acad. Sci. USA 92, 5446-5450 (1995).
10. Rohl, C.A., Chakrabartty, A. & Baldwin, R.L. Helix propagation and N-cap propensities of the amino acids measured in alanine-based peptides in 40 volume percent trifluoroethanol. Protein Sci. 5, 2623-2637 (1996).
11. Lesk, A.M. & Chothia, C. How different amino acid sequences determine similar protein structures: the structure and evolutionary dynamics of the globins. J. Mol. Biol. 136, 225-270 (1980).
12. Goto, Y., Takahashi, N. & Fink, A.L. Mechanism of acid-induced folding of proteins. Biochemistry 29, 3480-3488 (1990).
13. Santoro, M.M. & Bolen, D.W. Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl α-chymotrypsin using different denaturants. Biochemistry 27, 8063-8068 (1988).
14. Serrano, L., Kellis, J.T. Jr, Cann, P., Marouschek, A. & Fersht, A.R. The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. J. Mol. Biol. 224, 783-804 (see page 785) (1992).
15. Griko YV; Privalov PL. Thermodynamic puzzle of apomyoglobin unfolding. J. Mol. Biol. 235, 1318-1325 (1994).
16. Nishii, I., Kataoka, M. & Goto, Y. Thermodynamic stability of the molten globule states of apomyoglobin. J. Mol. Biol. 250, 223-238 (1995).
17. Richmond, T.J. & Richards, F.M. Packing of alpha-helices: geometrical constraints and contact areas. J. Mol. Biol. 119, 537-555 (1978).
18. Baldwin, R.L. How does protein folding get started? Trends Biochem. Sci. 14, 291-294 (1989).
19. Muñoz, V. & Serrano, L. Elucidating the folding problem of helical peptides using empirical parameters. Nature Struct. Biol. 1, 399-409 (1994).
20. Sambrook, J., Fritsch, E.F. & Maniatis, T. Molecular Cloning: a laboratory manual (Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, 1989).
21. Teale, F.W.J. Cleavage of the haem-protein link by acid methylethylketone. Biochim. Biophys. Acts. 35, 543-543 (1959).
22. Fanelli, A.R., Antonini, E. & Caputo, A. Studies on the structure of hemoglobin. I. Physicochemical properties of human globin. Biochim. Biophys. Acta. 30, 608-615 (1958).
23. Edelhoch, H. Spectroscopic determination of tryptophan and tyrosine in proteins. Biochemistry 6, 1948-1954 (1967).
24. Kraulis, P.J. Molscript - A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).