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Volumn 44, Issue 18, 2005, Pages 7013-7023

Cooperative sub-millisecond folding kinetics of apomyoglobin pH 4 intermediate

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; FLUORESCENCE; HYDROPHOBICITY; KINETIC THEORY; PH EFFECTS; PROBES;

EID: 18244401924     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047372v     Document Type: Article
Times cited : (19)

References (55)
  • 1
    • 0029904282 scopus 로고    scopus 로고
    • Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin
    • Jamin, M., and Baldwin, R. L. (1996) Refolding and unfolding kinetics of the equilibrium folding intermediate of apomyoglobin, Nat. Struct. Biol. 3, 613-618.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 613-618
    • Jamin, M.1    Baldwin, R.L.2
  • 2
    • 0032549072 scopus 로고    scopus 로고
    • Two forms of the pH 4 folding intermediate of apomyoglobin
    • Jamin, M., and Baldwin, R. L. (1998) Two forms of the pH 4 folding intermediate of apomyoglobin, J. Mol. Biol. 276, 491-504.
    • (1998) J. Mol. Biol. , vol.276 , pp. 491-504
    • Jamin, M.1    Baldwin, R.L.2
  • 3
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings, P. A., and Wright, P. E. (1993) Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin, Science 262, 892-896.
    • (1993) Science , vol.262 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2
  • 4
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson, F. M., Wright, P. E., and Baldwin, R. L. (1990) Structural characterization of a partly folded apomyoglobin intermediate, Science 249, 1544-1548.
    • (1990) Science , vol.249 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 5
    • 0842299585 scopus 로고    scopus 로고
    • Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness
    • Uzawa, T., Akiyama, S., Kimura, T., Takahashi, S., Ishimori, K., Morishima, I., and Fujisawa, T. (2004) Collapse and search dynamics of apomyoglobin folding revealed by submillisecond observations of alpha-helical content and compactness, Proc. Natl. Acad. Sci. U.S.A. 101, 1171-1176.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1171-1176
    • Uzawa, T.1    Akiyama, S.2    Kimura, T.3    Takahashi, S.4    Ishimori, K.5    Morishima, I.6    Fujisawa, T.7
  • 6
    • 0037188382 scopus 로고    scopus 로고
    • Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: Characterization of kinetic folding intermediates of apomyoglobin
    • Haruta, N., and Kitagawa, T. (2002) Time-resolved UV resonance Raman investigation of protein folding using a rapid mixer: characterization of kinetic folding intermediates of apomyoglobin, Biochemistry 41, 6595-6604.
    • (2002) Biochemistry , vol.41 , pp. 6595-6604
    • Haruta, N.1    Kitagawa, T.2
  • 7
    • 0031853168 scopus 로고    scopus 로고
    • Changes in side chain packing during apomyoglobin folding characterized by pulsed thioldisulfide exchange
    • Ha, J. H., and Loh, S. N. (1998) Changes in side chain packing during apomyoglobin folding characterized by pulsed thioldisulfide exchange, Nat. Struct. Biol. 5, 730-737.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 730-737
    • Ha, J.H.1    Loh, S.N.2
  • 8
    • 0036382667 scopus 로고    scopus 로고
    • The apomyoglobin folding pathway revisited: Structural heterogeneity in the kinetic burst phase intermediate
    • Nishimura, C., Dyson, H. J., and Wright, P. E. (2002) The apomyoglobin folding pathway revisited: structural heterogeneity in the kinetic burst phase intermediate, J. Mol. Biol. 322, 483-489.
    • (2002) J. Mol. Biol. , vol.322 , pp. 483-489
    • Nishimura, C.1    Dyson, H.J.2    Wright, P.E.3
  • 9
    • 0031932824 scopus 로고    scopus 로고
    • Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding
    • Eliezer, D., Yao, J., Dyson, H. J. and Wright, P. E. (1998) Structural and dynamic characterization of partially folded states of apomyoglobin and implications for protein folding, Nat. Struct. Biol. 5, 148-155.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 148-155
    • Eliezer, D.1    Yao, J.2    Dyson, H.J.3    Wright, P.E.4
  • 10
    • 0034696675 scopus 로고    scopus 로고
    • Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin
    • Eliezer, D., Chung, J., Dyson, H. J., and Wright, P. E. (2000) Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin, Biochemistry 39, 2894-2901.
    • (2000) Biochemistry , vol.39 , pp. 2894-2901
    • Eliezer, D.1    Chung, J.2    Dyson, H.J.3    Wright, P.E.4
  • 11
    • 0033600716 scopus 로고    scopus 로고
    • Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate
    • Jamin, M., Yeh, S. R., Rousseau, D. L., and Baldwin, R. L. (1999) Submillisecond unfolding kinetics of apomyoglobin and its pH 4 intermediate, J. Mol. Biol. 292, 731-740.
    • (1999) J. Mol. Biol. , vol.292 , pp. 731-740
    • Jamin, M.1    Yeh, S.R.2    Rousseau, D.L.3    Baldwin, R.L.4
  • 12
    • 0014718113 scopus 로고
    • Protein denaturation. Part C. Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970) Protein denaturation. Part C. Theoretical models for the mechanism of denaturation, Adv. Prot. Chem. 24, 2-95.
    • (1970) Adv. Prot. Chem. , vol.24 , pp. 2-95
    • Tanford, C.1
  • 13
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition
    • Jackson, S. E., and Fersht, A. R. (1991) Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition, Biochemistry 30, 10428-10435.
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 14
    • 0002343673 scopus 로고
    • Measuring the conformational stability of a protein
    • Creighton, T. E., Ed. IRL Press, Oxford, UK
    • Pace, C. N., Shirley, B. A. and Thompson, J. A. (1989) Measuring the conformational stability of a protein, in Protein Structure: A Practical Approach (Creighton, T. E., Ed.) pp 311-330, IRL Press, Oxford, UK.
    • (1989) Protein Structure: A Practical Approach , pp. 311-330
    • Pace, C.N.1    Shirley, B.A.2    Thompson, J.A.3
  • 15
    • 49749194276 scopus 로고
    • Studies on the structure of hemoglobin. I. Physicochemical properties of human globin
    • Fanelli, A. R., Antonini, E. and Caputo, A. (1958) Studies on the structure of hemoglobin. I. Physicochemical properties of human globin, Biochim. Biophys. Acta 30, 608-615.
    • (1958) Biochim. Biophys. Acta , vol.30 , pp. 608-615
    • Fanelli, A.R.1    Antonini, E.2    Caputo, A.3
  • 16
    • 0023462496 scopus 로고
    • High-level expression of sperm whale myoglobin in Escherichia coli
    • Springer, B. A. and Sligar, S. G. (1987) High-level expression of sperm whale myoglobin in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 84, 8961-8965.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8961-8965
    • Springer, B.A.1    Sligar, S.G.2
  • 17
    • 0029400889 scopus 로고
    • Overexpression of myoglobin and assignment of its amide, C alpha and C beta resonances
    • Jennings, P. A., Stone, M. J., and Wright, P. E. (1995) Overexpression of myoglobin and assignment of its amide, C alpha and C beta resonances, J. Biomol. NMR 6, 271-276.
    • (1995) J. Biomol. NMR , vol.6 , pp. 271-276
    • Jennings, P.A.1    Stone, M.J.2    Wright, P.E.3
  • 18
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins, Biochemistry 6, 1948-1954.
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 19
    • 0018450898 scopus 로고
    • Measurement of the dead time of a fluorescence stopped-flow instrument
    • Peterman, B. F. (1979) Measurement of the dead time of a fluorescence stopped-flow instrument, Anal. Biochem. 93, 442-444.
    • (1979) Anal. Biochem. , vol.93 , pp. 442-444
    • Peterman, B.F.1
  • 21
    • 0023697408 scopus 로고
    • Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants
    • Santoro, M. M., and Bolen, D. W. (1988) Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants, Biochemistry 27, 8063-8068.
    • (1988) Biochemistry , vol.27 , pp. 8063-8068
    • Santoro, M.M.1    Bolen, D.W.2
  • 22
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod, J., Wyman, J. and Changeux, J. P. (1965) On the nature of allosteric transitions: A plausible model, J. Mol. Biol. 12, 88-118.
    • (1965) J. Mol. Biol. , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 24
    • 0032568639 scopus 로고    scopus 로고
    • Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate
    • Kay, M. S., and Baldwin, R. L. (1998) Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate, Biochemistry 37, 7859-7868.
    • (1998) Biochemistry , vol.37 , pp. 7859-7868
    • Kay, M.S.1    Baldwin, R.L.2
  • 25
    • 0000269163 scopus 로고    scopus 로고
    • Case study 1: The folding process of apomyoglobin
    • Pain, R. H., Ed. Oxford University Press, Oxford, UK
    • Wright, P. E., and Baldwin, R. L. (2000) Case study 1: The folding process of apomyoglobin, in Mechanisms of Protein Folding (Pain, R. H., Ed.) pp 309-329, Oxford University Press, Oxford, UK.
    • (2000) Mechanisms of Protein Folding , pp. 309-329
    • Wright, P.E.1    Baldwin, R.L.2
  • 26
    • 18244386288 scopus 로고    scopus 로고
    • Apomyoglobin folding process
    • in press
    • Jamin, M. (2005) Apomyoglobin folding process, Prot. Pept. Lett., in press.
    • (2005) Prot. Pept. Lett.
    • Jamin, M.1
  • 27
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka, M., Nishii, I., Fujisawa, T., Ueki, T., Tokunaga, F., and Goto, Y. (1995) Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering, J. Mol. Biol. 249, 215-228.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 28
    • 0029014386 scopus 로고
    • Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway
    • Loh, S. N., Kay, M. S., and Baldwin, R. L. (1995) Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway, Proc. Natl. Acad. Sci. U.S.A. 92, 5446-5450.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 5446-5450
    • Loh, S.N.1    Kay, M.S.2    Baldwin, R.L.3
  • 29
    • 0034687084 scopus 로고    scopus 로고
    • Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue
    • Garcia, C., Nishimura, C., Cavagnero, S., Dyson, H. J., and Wright, P. E. (2000) Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue, Biochemistry 39, 11227-11237.
    • (2000) Biochemistry , vol.39 , pp. 11227-11237
    • Garcia, C.1    Nishimura, C.2    Cavagnero, S.3    Dyson, H.J.4    Wright, P.E.5
  • 30
    • 0029112554 scopus 로고
    • Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form
    • Kiefhaber, T., and Baldwin, R. L. (1995) Intrinsic stability of individual alpha helices modulates structure and stability of the apomyoglobin molten globule form, J. Mol. Biol. 252, 122-132.
    • (1995) J. Mol. Biol. , vol.252 , pp. 122-132
    • Kiefhaber, T.1    Baldwin, R.L.2
  • 31
    • 0032901420 scopus 로고    scopus 로고
    • Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through and obligatory intermediate
    • Tsui, V., Garcia, C., Cavagnero, S., Siuzdak, G., Dyson, H. J., and Wright, P. E. (1999) Quench-flow experiments combined with mass spectrometry show apomyoglobin folds through and obligatory intermediate, Protein Sci. 8, 45-49.
    • (1999) Protein Sci. , vol.8 , pp. 45-49
    • Tsui, V.1    Garcia, C.2    Cavagnero, S.3    Siuzdak, G.4    Dyson, H.J.5    Wright, P.E.6
  • 32
    • 0029278913 scopus 로고
    • Protein folding. An unfolding story
    • Creighton, T. E. (1995) Protein folding. An unfolding story, Curr. Biol. 5, 353-356.
    • (1995) Curr. Biol. , vol.5 , pp. 353-356
    • Creighton, T.E.1
  • 33
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov, P. L. (1979) Stability of proteins: small globular proteins, Adv. Prot. Chem. 33, 167-241.
    • (1979) Adv. Prot. Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 34
    • 0028329347 scopus 로고
    • Thermodynamic puzzle of apomyoglobin unfolding
    • Griko, Y. V., and Privalov, P. L. (1994) Thermodynamic puzzle of apomyoglobin unfolding, J. Mol. Biol. 235, 1318-1325.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1318-1325
    • Griko, Y.V.1    Privalov, P.L.2
  • 35
    • 0033864682 scopus 로고    scopus 로고
    • The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry
    • Jamin, M., Antalik, M., Loh, S. N., Bolen, D. W., and Baldwin, R. L. (2000) The unfolding enthalpy of the pH 4 molten globule of apomyoglobin measured by isothermal titration calorimetry, Protein. Sci. 9, 1340-1346.
    • (2000) Protein. Sci. , vol.9 , pp. 1340-1346
    • Jamin, M.1    Antalik, M.2    Loh, S.N.3    Bolen, D.W.4    Baldwin, R.L.5
  • 36
    • 0029132790 scopus 로고
    • Thermodynamics of partly folded intermediates in proteins
    • Freire, E. (1995) Thermodynamics of partly folded intermediates in proteins, Annu. Rev. Biophys. Biomol. Struct. 24, 141-165.
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 141-165
    • Freire, E.1
  • 37
    • 0028243107 scopus 로고
    • Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
    • Nishii, I., Kataoka, M., Tokunaga, F., and Goto, Y. (1994) Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding, Biochemistry 33, 4903-4909.
    • (1994) Biochemistry , vol.33 , pp. 4903-4909
    • Nishii, I.1    Kataoka, M.2    Tokunaga, F.3    Goto, Y.4
  • 38
    • 0029981924 scopus 로고    scopus 로고
    • Packing interactions in the apomyglobin folding intermediate
    • Kay, M. S., and Baldwin, R. L. (1996) Packing interactions in the apomyglobin folding intermediate, Nat. Struct. Biol. 3, 439-445.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 439-445
    • Kay, M.S.1    Baldwin, R.L.2
  • 39
    • 0030694241 scopus 로고    scopus 로고
    • Coopetativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations
    • Luo, Y., Kay, M. S., and Baldwin, R. L. (1997) Coopetativity of folding of the apomyoglobin pH 4 intermediate studied by glycine and proline mutations, Nat. Struct. Biol. 4, 925-930.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 925-930
    • Luo, Y.1    Kay, M.S.2    Baldwin, R.L.3
  • 40
    • 0015505381 scopus 로고
    • A sequential model of nucleation-dependent protein folding: Kinetic studies of ribonuclease A
    • Tsong, T. Y., and Baldwin, R. L. (1972) A sequential model of nucleation-dependent protein folding: kinetic studies of ribonuclease A, J. Mol. Biol. 63, 453-469.
    • (1972) J. Mol. Biol. , vol.63 , pp. 453-469
    • Tsong, T.Y.1    Baldwin, R.L.2
  • 41
    • 0034725549 scopus 로고    scopus 로고
    • A statistical appraisal of native state hydrogen exchange data: Evidence for a burst phase continuum?
    • Parker, M. J., and Marqusee, S. (2000) A statistical appraisal of native state hydrogen exchange data: evidence for a burst phase continuum?, J. Mol. Biol. 300, 1361-1375.
    • (2000) J. Mol. Biol. , vol.300 , pp. 1361-1375
    • Parker, M.J.1    Marqusee, S.2
  • 42
    • 0028802181 scopus 로고
    • Initial hydrophobic collapse in the folding of barstar
    • Agashe, V. R., Shastry, M. C. R., and Udgaonkar, J. B. (1995) Initial hydrophobic collapse in the folding of barstar, Nature 377, 754-757.
    • (1995) Nature , vol.377 , pp. 754-757
    • Agashe, V.R.1    Shastry, M.C.R.2    Udgaonkar, J.B.3
  • 44
    • 0347284262 scopus 로고    scopus 로고
    • Rapid collapse precedes the fast two-state folding of the cold shock protein
    • Magg, C., and Schmid, F. X. (2004) Rapid collapse precedes the fast two-state folding of the cold shock protein, J. Mol. Biol. 335, 1309-1323.
    • (2004) J. Mol. Biol. , vol.335 , pp. 1309-1323
    • Magg, C.1    Schmid, F.X.2
  • 45
    • 0034714154 scopus 로고    scopus 로고
    • Two-state expansion and collapse of a polypeptide
    • Hagen, S. J., and Eaton, W. A. (2000) Two-state expansion and collapse of a polypeptide, J. Mol. Biol. 301, 1019-1027.
    • (2000) J. Mol. Biol. , vol.301 , pp. 1019-1027
    • Hagen, S.J.1    Eaton, W.A.2
  • 46
    • 0037007487 scopus 로고    scopus 로고
    • Test for cooperativity in the early kinetic intermediate in lysozyme folding
    • Bachmann, A., Segel, D., and Kiefhaber, T. (2002) Test for cooperativity in the early kinetic intermediate in lysozyme folding, Biophys. Chem. 96, 141-151.
    • (2002) Biophys. Chem. , vol.96 , pp. 141-151
    • Bachmann, A.1    Segel, D.2    Kiefhaber, T.3
  • 47
    • 0026330844 scopus 로고
    • Calorimetric determination of the energetics of the molten globule intermediate in protein folding: Apo-alpha-lactalbumin
    • Xie, D., Bhakuni, V., and Freire, E. (1991) Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-alpha-lactalbumin, Biochemistry 30, 10673-10678.
    • (1991) Biochemistry , vol.30 , pp. 10673-10678
    • Xie, D.1    Bhakuni, V.2    Freire, E.3
  • 48
    • 0029765444 scopus 로고    scopus 로고
    • Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology
    • Schulman, B. A., and Kim, P. S. (1996) Proline scanning mutagenesis of a molten globule reveals non-cooperative formation of a protein's overall topology, Nat. Struct. Biol. 3, 682-687.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 682-687
    • Schulman, B.A.1    Kim, P.S.2
  • 49
    • 0030768045 scopus 로고    scopus 로고
    • A residue-specific NMR view of the non-cooperative unfolding of a molten globule
    • Schulman, B. A., Kim, P. S., Dobson, C. M. and Redfield, C. (1997) A residue-specific NMR view of the non-cooperative unfolding of a molten globule, Nat. Struct. Biol. 4, 630-634.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 630-634
    • Schulman, B.A.1    Kim, P.S.2    Dobson, C.M.3    Redfield, C.4
  • 50
  • 51
    • 0033613115 scopus 로고    scopus 로고
    • The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding
    • Luo, Y., & Baldwin, R. L. (1999) The 28-111 disulfide bond constrains the alpha-lactalbumin molten globule and weakens its cooperativity of folding, Proc. Natl. Acad. Sci. U.S.A. 96, 11283-11287.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 11283-11287
    • Luo, Y.1    Baldwin, R.L.2
  • 52
    • 0033514920 scopus 로고    scopus 로고
    • Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate
    • Kay, M. S., Ramos, C. H., and Baldwin, R. L. (1999) Specificity of native-like interhelical hydrophobic contacts in the apomyoglobin intermediate, Proc. Natl. Acad. Sci. U.S.A. 96, 2007-2012.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2007-2012
    • Kay, M.S.1    Ramos, C.H.2    Baldwin, R.L.3
  • 53
    • 0032067753 scopus 로고    scopus 로고
    • The core of apomyoglobin E-form folds at the diffusion limit
    • Gilmanshin, R., Callender, R. H., and Dyer, R. B. (1998) The core of apomyoglobin E-form folds at the diffusion limit, Nat. Struct. Biol. 5, 363-365.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 363-365
    • Gilmanshin, R.1    Callender, R.H.2    Dyer, R.B.3
  • 54
    • 0035339911 scopus 로고    scopus 로고
    • Core formation in apomyoglobin: Probing the upper reaches of the folding energy landscape
    • Gulotta, M., Gilmanshin, R., Buscher, T. C., Callender, R. H., and Dyer, R. B. (2001) Core formation in apomyoglobin: probing the upper reaches of the folding energy landscape, Biochemistry 40, 5137-5143.
    • (2001) Biochemistry , vol.40 , pp. 5137-5143
    • Gulotta, M.1    Gilmanshin, R.2    Buscher, T.C.3    Callender, R.H.4    Dyer, R.B.5


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