메뉴 건너뛰기




Volumn 324, Issue 2, 2002, Pages 331-347

Differential salt-induced stabilization of structure in the initial folding intermediate ensemble of barstar

Author keywords

Burst phase intermediate; Hofmeister effect; Protein electrostatics; Protein folding; Salt induced protein stabilization

Indexed keywords

BARSTAR; MAGNESIUM CHLORIDE; POTASSIUM CHLORIDE; TRYPTOPHAN; UREA;

EID: 0036438892     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01068-9     Document Type: Article
Times cited : (42)

References (74)
  • 1
    • 0031697733 scopus 로고    scopus 로고
    • The burst phase in ribonuclease A folding and solvent dependence of the unfolded state
    • Qi, P. X., Sosnick, T. R. & Englander, S. W. (1998). The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nature Struct. Biol. 5, 882-884.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 882-884
    • Qi, P.X.1    Sosnick, T.R.2    Englander, S.W.3
  • 3
    • 0002982949 scopus 로고    scopus 로고
    • Relevance of burst phase changes in optical signals of polypeptides during protein folding
    • Vijayan, M., Yathindra, N. & Kolaskar, A. S., eds, Universities Press, Hyderabad
    • Bhuyan, A. K. & Udgaonkar, J. B. (1999). Relevance of burst phase changes in optical signals of polypeptides during protein folding. In Perspectives in Structural Biology (Vijayan, M., Yathindra, N. & Kolaskar, A. S., eds), pp. 293, Universities Press, Hyderabad.
    • (1999) Perspectives in Structural Biology , pp. 293
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 5
    • 0031919973 scopus 로고    scopus 로고
    • Evidence for barrier-limited protein folding kinetics on the microsecond time scale
    • Shastry, M. C. R. & Roder, H. (1998). Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nature Struct. Biol. 5, 385-392.
    • (1998) Nature Struct. Biol. , vol.5 , pp. 385-392
    • Shastry, M.C.R.1    Roder, H.2
  • 6
    • 0028901085 scopus 로고
    • The folding mechanism of barstar: Evidence for multiple pathways and multiple intermediates
    • Shastry, M. C. R. & Udgaonkar, J. B. (1995). The folding mechanism of barstar: Evidence for multiple pathways and multiple intermediates. J. Mol. Biol. 247, 1013-1027.
    • (1995) J. Mol. Biol. , vol.247 , pp. 1013-1027
    • Shastry, M.C.R.1    Udgaonkar, J.B.2
  • 7
    • 0032499639 scopus 로고    scopus 로고
    • Characterization of collapsed states in the early stages of the refolding of hen lysozyme
    • Morgan, C. L., Miranker, A. & Dobson, C. M. (1998). Characterization of collapsed states in the early stages of the refolding of hen lysozyme. Biochemistry, 37, 8473-8480.
    • (1998) Biochemistry , vol.37 , pp. 8473-8480
    • Morgan, C.L.1    Miranker, A.2    Dobson, C.M.3
  • 8
    • 0029738416 scopus 로고    scopus 로고
    • Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A
    • Houry, W. A., Rothwarf, D. M. & Scheraga, H. A. (1996). Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A. Biochemistry, 35, 10125-10133.
    • (1996) Biochemistry , vol.35 , pp. 10125-10133
    • Houry, W.A.1    Rothwarf, D.M.2    Scheraga, H.A.3
  • 9
    • 0029811091 scopus 로고    scopus 로고
    • Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange
    • Houry, W. A. & Scheraga, H. A. (1996). Structure of a hydrophobically collapsed intermediate on the conformational folding pathway of ribonuclease A probed by hydrogen-deuterium exchange. Biochemistry, 35, 11734-11746.
    • (1996) Biochemistry , vol.35 , pp. 11734-11746
    • Houry, W.A.1    Scheraga, H.A.2
  • 11
    • 0036382667 scopus 로고    scopus 로고
    • The apomyoglobin folding pathway revisited: Structural heterogeneity in the kinetic burst phase intermediate
    • Nishimura, C., Jane Dyson, H. & Wright, P. (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    Jane Dyson, H.2    Wright, P.3
  • 12
    • 0033551522 scopus 로고    scopus 로고
    • Observation of multistate kinetics during the slow folding and unfolding of barstar
    • Bhuyan, A. K. & Udgaonkar, J. B. (1999). Observation of multistate kinetics during the slow folding and unfolding of barstar. Biochemistry, 38, 9158-9168.
    • (1999) Biochemistry , vol.38 , pp. 9158-9168
    • Bhuyan, A.K.1    Udgaonkar, J.B.2
  • 13
    • 0021525532 scopus 로고
    • Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state
    • Segawa, S. & Sugihara, M. (1984). Characterization of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions on the transition state. Biopolymers, 23, 2473-2488.
    • (1984) Biopolymers , vol.23 , pp. 2473-2488
    • Segawa, S.1    Sugihara, M.2
  • 14
    • 0024596024 scopus 로고
    • 2+ binding on the folding kinetics of alpha-lactalbumin
    • 2+ binding on the folding kinetics of alpha-lactalbumin. J. Mol. Biol. 206, 547-561.
    • (1989) J. Mol. Biol. , vol.206 , pp. 547-561
    • Kuwajima, K.1    Mitani, M.2    Sugai, S.3
  • 15
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chen, B. L., Baase, W. A. & Schellman, J. A. (1989). Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry, 28, 691-699.
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chen, B.L.1    Baase, W.A.2    Schellman, J.A.3
  • 16
    • 0026545583 scopus 로고
    • Folding kinetics of T4 lysozyme and nine mutants at 12°C
    • Chen, B. L., Baase, W. A., Nicholson, H. & Schellman, J. A. (1992). Folding kinetics of T4 lysozyme and nine mutants at 12°C. Biochemistry, 31, 1464-1476.
    • (1992) Biochemistry , vol.31 , pp. 1464-1476
    • Chen, B.L.1    Baase, W.A.2    Nicholson, H.3    Schellman, J.A.4
  • 17
    • 0028271856 scopus 로고
    • Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase
    • Chen, X. & Matthews, C. R. (1994). Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase. Biochemistry, 33, 6356-6362.
    • (1994) Biochemistry , vol.33 , pp. 6356-6362
    • Chen, X.1    Matthews, C.R.2
  • 18
    • 0028981210 scopus 로고
    • Negative activation enthalpies in the kinetics of protein folding
    • Oliveberg, M., Tan, Y. J. & Fersht, A. R. (1995). Negative activation enthalpies in the kinetics of protein folding. Proc. Natl. Acad. Sci. USA, 92, 8926-8929.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.J.2    Fersht, A.R.3
  • 19
    • 0030606223 scopus 로고    scopus 로고
    • Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways
    • Tan, Y. J., Oliveberg, M. & Fersht, A. R. (1996). Titration properties and thermodynamics of the transition state for folding: Comparison of two-state and multi-state folding pathways. J. Mol. Biol. 264, 377-389.
    • (1996) J. Mol. Biol. , vol.264 , pp. 377-389
    • Tan, Y.J.1    Oliveberg, M.2    Fersht, A.R.3
  • 20
    • 0030882667 scopus 로고    scopus 로고
    • Thermodynamics of the complex protein unfolding reaction of barstar
    • Agashe, V. R., Schmid, F. X. & Udgaonkar, J. B. (1997). Thermodynamics of the complex protein unfolding reaction of barstar. Biochemistry, 36, 12288-12295.
    • (1997) Biochemistry , vol.36 , pp. 12288-12295
    • Agashe, V.R.1    Schmid, F.X.2    Udgaonkar, J.B.3
  • 21
    • 0001679156 scopus 로고
    • The effects of neutral salts on the structure and conformational stability of macromolecules in solution
    • Timasheff, S. N. & Fasman, G. D., eds, Marcel Dekker, New York
    • von Hippel, P. H. & Schleich, T. (1969). The effects of neutral salts on the structure and conformational stability of macromolecules in solution. In Structure and Stability of Biological Macromolecules (Timasheff, S. N. & Fasman, G. D., eds), pp. 417, Marcel Dekker, New York.
    • (1969) Structure and Stability of Biological Macromolecules , pp. 417
    • Von Hippel, P.H.1    Schleich, T.2
  • 22
    • 0027433511 scopus 로고
    • Intermediate conformational states of apocytochrome c
    • Hamada, D., Hoshino, M., Kataoka, M., Fink, A. L. & Goto, Y. (1993). Intermediate conformational states of apocytochrome c. Biochemistry, 32, 10351-10358.
    • (1993) Biochemistry , vol.32 , pp. 10351-10358
    • Hamada, D.1    Hoshino, M.2    Kataoka, M.3    Fink, A.L.4    Goto, Y.5
  • 23
    • 0032525256 scopus 로고    scopus 로고
    • Anion-induced folding of Staphylococcal nuclease: Characterization of multiple equilibrium partially folded intermediates
    • Uversky, V. N., Karnoup, A. S., Segel, D. J., Seshadri, S., Doniach, S. & Fink, A. L. (1998). Anion-induced folding of Staphylococcal nuclease: Characterization of multiple equilibrium partially folded intermediates. J. Mol. Biol. 278, 879-894.
    • (1998) J. Mol. Biol. , vol.278 , pp. 879-894
    • Uversky, V.N.1    Karnoup, A.S.2    Segel, D.J.3    Seshadri, S.4    Doniach, S.5    Fink, A.L.6
  • 24
    • 0033592403 scopus 로고    scopus 로고
    • A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding
    • Bieri, O., Wildegger, G., Bachmann, A., Wagner, C. & Kiefhaber, T. (1999). A salt-induced kinetic intermediate is on a new parallel pathway of lysozyme folding. Biochemistry, 38, 12460-12470.
    • (1999) Biochemistry , vol.38 , pp. 12460-12470
    • Bieri, O.1    Wildegger, G.2    Bachmann, A.3    Wagner, C.4    Kiefhaber, T.5
  • 25
    • 0032718386 scopus 로고    scopus 로고
    • Salt-induced detour through compact regions of the protein folding landscape
    • Otzen, D. E. & Oliveberg, M. (1999). Salt-induced detour through compact regions of the protein folding landscape. Proc. Natl. Acad. Sci. USA, 96, 11746-11751.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11746-11751
    • Otzen, D.E.1    Oliveberg, M.2
  • 26
    • 0030787174 scopus 로고    scopus 로고
    • Multiple intermediates and transition states during protein unfolding
    • Zaidi, F. N., Nath, U. & Udgaonkar, J. B. (1997). Multiple intermediates and transition states during protein unfolding. Nature Struct. Biol. 4, 1016-1024.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 1016-1024
    • Zaidi, F.N.1    Nath, U.2    Udgaonkar, J.B.3
  • 27
    • 0027385015 scopus 로고
    • The refolding of cis- and trans-peptidylprolyl isomers of barstar
    • Schreiber, G. & Fersht, A. R. (1993). The refolding of cis- and trans-peptidylprolyl isomers of barstar. Biochemistry, 32, 11195-11203.
    • (1993) Biochemistry , vol.32 , pp. 11195-11203
    • Schreiber, G.1    Fersht, A.R.2
  • 28
    • 0028072360 scopus 로고
    • Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone
    • Shastry, M. C. R., Agashe, V. R. & Udgaonkar, J. B. (1994). Quantitative analysis of the kinetics of denaturation and renaturation of barstar in the folding transition zone. Protein Sci. 3, 1409-1417.
    • (1994) Protein Sci. , vol.3 , pp. 1409-1417
    • Shastry, M.C.R.1    Agashe, V.R.2    Udgaonkar, J.B.3
  • 29
    • 0028947236 scopus 로고
    • Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride
    • Agashe, V. R. & Udgaonkar, J. B. (1995). Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride. Biochemistry, 34, 3286-3299.
    • (1995) Biochemistry , vol.34 , pp. 3286-3299
    • Agashe, V.R.1    Udgaonkar, J.B.2
  • 30
    • 0034665642 scopus 로고    scopus 로고
    • The slow folding reaction of barstar: The core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain
    • Sridevi, K., Juneja, J., Bhuyan, A. K., Krishnamoorthy, G. & Udgaonkar, J. B. (2000). The slow folding reaction of barstar: The core tryptophan region attains tight packing before substantial secondary and tertiary structure formation and final compaction of the polypeptide chain. J. Mol. Biol. 302, 479-495.
    • (2000) J. Mol. Biol. , vol.302 , pp. 479-495
    • Sridevi, K.1    Juneja, J.2    Bhuyan, A.K.3    Krishnamoorthy, G.4    Udgaonkar, J.B.5
  • 31
    • 0028802181 scopus 로고
    • Initial hydrophobic collapse in the folding of barstar
    • Agashe, V. R., Shastry, M. C. R. & 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
  • 32
    • 0035909818 scopus 로고    scopus 로고
    • pH-jump-induced folding and unfolding studies of barstar: Evidence for multiple folding and unfolding pathways
    • Rami, B. R. & Udgaonkar, J. B. (2001). pH-jump-induced folding and unfolding studies of barstar: Evidence for multiple folding and unfolding pathways. Biochemistry, 40, 15267-15279.
    • (2001) Biochemistry , vol.40 , pp. 15267-15279
    • Rami, B.R.1    Udgaonkar, J.B.2
  • 33
    • 0037065672 scopus 로고    scopus 로고
    • Mechanism of formation of a productive molten globule form of barstar
    • Rami, B. R. & Udgaonkar, J. B. (2002). Mechanism of formation of a productive molten globule form of barstar. Biochemistry, 41, 1710-1716.
    • (2002) Biochemistry , vol.41 , pp. 1710-1716
    • Rami, B.R.1    Udgaonkar, J.B.2
  • 34
    • 34247513828 scopus 로고
    • Zur lehre von der wirkung der salze. Zweite mittheilung
    • Hofmeister, F. (1888). Zur lehre von der wirkung der salze. Zweite mittheilung. Arch. Expt. Pathol. Pharmakol. 24, 247-260.
    • (1888) Arch. Expt. Pathol. Pharmakol. , vol.24 , pp. 247-260
    • Hofmeister, F.1
  • 35
    • 0034620528 scopus 로고    scopus 로고
    • Rational modification of protein stability by the mutation of charged surface residues
    • Spector, S., Wang, M., Carp, S. A., Robblee, J., Hendsch, Z. S., Fairman, R. et al. (2000). Rational modification of protein stability by the mutation of charged surface residues. Biochemistry, 39, 872-879.
    • (2000) Biochemistry , vol.39 , pp. 872-879
    • Spector, S.1    Wang, M.2    Carp, S.A.3    Robblee, J.4    Hendsch, Z.S.5    Fairman, R.6
  • 37
    • 0034100848 scopus 로고    scopus 로고
    • Two exposed amino acid residues confer thermostability on a cold shock protein
    • Perl, D., Mueller, U., Heinemann, U. & Schmid, F. X. (2000). Two exposed amino acid residues confer thermostability on a cold shock protein. Nature Struct. Biol. 7, 380-383.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 380-383
    • Perl, D.1    Mueller, U.2    Heinemann, U.3    Schmid, F.X.4
  • 38
    • 0033554840 scopus 로고    scopus 로고
    • Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface
    • Loladze, V. V., Ibarra-Molero, B., Sanchez-Ruiz, J. M. & Makhatadze, G. I. (1999). Engineering a thermostable protein via optimization of charge-charge interactions on the protein surface. Biochemistry, 38, 16419-16423.
    • (1999) Biochemistry , vol.38 , pp. 16419-16423
    • Loladze, V.V.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3    Makhatadze, G.I.4
  • 39
    • 0028126676 scopus 로고
    • Optimization of the electrostatic interactions in proteins of different functional and folding type
    • Spassov, V. Z., Karshikoff, A. D. & Ladenstein, R. (1994). Optimization of the electrostatic interactions in proteins of different functional and folding type. Protein Sci. 3, 1556-1569.
    • (1994) Protein Sci. , vol.3 , pp. 1556-1569
    • Spassov, V.Z.1    Karshikoff, A.D.2    Ladenstein, R.3
  • 41
    • 0033539662 scopus 로고    scopus 로고
    • Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH
    • Uversky, V. N., Gillespie, J. R., Millett, I. S., Khodyakova, A. V., Vasiliev, A. M., Chernovskaya, T. V. et al. (1999). Natively unfolded human prothymosin alpha adopts partially folded collapsed conformation at acidic pH. Biochemistry, 38, 15009-15016.
    • (1999) Biochemistry , vol.38 , pp. 15009-15016
    • Uversky, V.N.1    Gillespie, J.R.2    Millett, I.S.3    Khodyakova, A.V.4    Vasiliev, A.M.5    Chernovskaya, T.V.6
  • 42
    • 0033777462 scopus 로고    scopus 로고
    • The acid-induced folded state of Sac7d is the native state
    • Bedell, J. L., McCrary, B. S., Edmondson, S. P. & Shriver, J. W. (2000). The acid-induced folded state of Sac7d is the native state. Protein Sci. 9, 1878-1888.
    • (2000) Protein Sci. , vol.9 , pp. 1878-1888
    • Bedell, J.L.1    McCrary, B.S.2    Edmondson, S.P.3    Shriver, J.W.4
  • 43
    • 0034769732 scopus 로고    scopus 로고
    • Salt-dependent monomerdimer equilibrium of bovine beta-lactoglobulin at pH 3
    • Sakurai, K., Oobatake, M. & Goto, Y. (2001). Salt-dependent monomerdimer equilibrium of bovine beta-lactoglobulin at pH 3. Protein Sci. 10, 2325-2335.
    • (2001) Protein Sci. , vol.10 , pp. 2325-2335
    • Sakurai, K.1    Oobatake, M.2    Goto, Y.3
  • 44
    • 0028774340 scopus 로고
    • Stability and function: Two constraints in the evolution of barstar and other proteins
    • Schreiber, G., Buckle, A. M. & Fersht, A. R. (1994). Stability and function: Two constraints in the evolution of barstar and other proteins. Structure, 2, 945-951.
    • (1994) Structure , vol.2 , pp. 945-951
    • Schreiber, G.1    Buckle, A.M.2    Fersht, A.R.3
  • 45
    • 0035964254 scopus 로고    scopus 로고
    • Stabilization of a fibronectin type III domain by the removal of unfavourable electrostatic interactions on the protein surface
    • Koide, A., Jordan, M. R., Horner, S. R., Batori, V. & Koide, S. (2001). Stabilization of a fibronectin type III domain by the removal of unfavourable electrostatic interactions on the protein surface. Biochemistry, 40, 10326-10333.
    • (2001) Biochemistry , vol.40 , pp. 10326-10333
    • Koide, A.1    Jordan, M.R.2    Horner, S.R.3    Batori, V.4    Koide, S.5
  • 47
    • 0003388018 scopus 로고
    • Electrostatic interactions
    • Jencks, W. P., ed., Dover, New York
    • Jencks, W. P. (1987). Electrostatic interactions. In Catalysis in Chemistry and Enzymology (Jencks, W. P., ed.), pp. 351, Dover, New York.
    • (1987) Catalysis in Chemistry and Enzymology , pp. 351
    • Jencks, W.P.1
  • 48
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects. Hofmeister effects, and osmotic effects of salts
    • Record, M. T., Jr, Zhang, W. & Anderson, C. F. (1998). Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects. Hofmeister effects, and osmotic effects of salts. Advan. Protein Chem. 51, 281-353.
    • (1998) Advan. Protein Chem. , vol.51 , pp. 281-353
    • Record M.T., Jr.1    Zhang, W.2    Anderson, C.F.3
  • 49
    • 0029792830 scopus 로고    scopus 로고
    • How Hofmeister ion interactions affect protein stability
    • Baldwin, R. L. (1996). How Hofmeister ion interactions affect protein stability. Biophys. J. 71, 2056-2063.
    • (1996) Biophys. J. , vol.71 , pp. 2056-2063
    • Baldwin, R.L.1
  • 50
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition
    • von Hippel, P. H. & Wong, K. Y. (1965). On the conformational stability of globular proteins. The effects of various electrolytes and nonelectrolytes on the thermal ribonuclease transition. J. Biol. Chem. 240, 3909-3923.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3909-3923
    • Von Hippel, P.H.1    Wong, K.Y.2
  • 51
    • 0022147096 scopus 로고
    • The Hofmeister effect and the behaviour of water at interfaces
    • Collins, K. D. & Washabaugh, M. W. (1985). The Hofmeister effect and the behaviour of water at interfaces. Quart. Rev. Biophys. 18, 323-422.
    • (1985) Quart. Rev. Biophys. , vol.18 , pp. 323-422
    • Collins, K.D.1    Washabaugh, M.W.2
  • 52
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff, S. N. (1993). The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22, 67-97.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 53
    • 0025030410 scopus 로고
    • A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures
    • Schellman, J. A. (1990). A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures. Biophys. Chem. 37, 121-140.
    • (1990) Biophys. Chem. , vol.37 , pp. 121-140
    • Schellman, J.A.1
  • 54
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman, J. (1964). Linked functions and reciprocal effects in hemoglobin: A second look. Advan. Protein Chem. 19, 223-286.
    • (1964) Advan. Protein Chem. , vol.19 , pp. 223-286
    • Wyman, J.1
  • 55
    • 0028618410 scopus 로고
    • Ontribution of the surface free energy perturbation to protein-solvent interactions
    • Kita, Y., Arakawa, T., Lin, T. Y. & Timasheff, S. N. (1994). Ontribution of the surface free energy perturbation to protein-solvent interactions. Biochemistry, 33, 15178-15189.
    • (1994) Biochemistry , vol.33 , pp. 15178-15189
    • Kita, Y.1    Arakawa, T.2    Lin, T.Y.3    Timasheff, S.N.4
  • 56
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salts in concentrated solutions
    • Arakawa, T. & Timasheff, S. N. (1982). Preferential interactions of proteins with salts in concentrated solutions. Biochemistry, 21, 6545-6552.
    • (1982) Biochemistry , vol.21 , pp. 6545-6552
    • Arakawa, T.1    Timasheff, S.N.2
  • 57
    • 0021755248 scopus 로고
    • Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding
    • Arakawa, T. & Timasheff, S. N. (1984). Mechanism of protein salting in and salting out by divalent cation salts: Balance between hydration and salt binding. Biochemistry, 23, 5912-5923.
    • (1984) Biochemistry , vol.23 , pp. 5912-5923
    • Arakawa, T.1    Timasheff, S.N.2
  • 58
    • 0027240046 scopus 로고
    • Stabilization of a protein by guanidinium chloride
    • Mayr, L. M. & Schmid, F. X. (1993). Stabilization of a protein by guanidinium chloride. Biochemistry, 32, 7994-7998.
    • (1993) Biochemistry , vol.32 , pp. 7994-7998
    • Mayr, L.M.1    Schmid, F.X.2
  • 60
    • 0028132243 scopus 로고
    • Thermal unfolding of tetrameric melittin: Comparison with the molten globule state of cytochrome c
    • Hagihara, Y., Oobatake, M. & Goto, Y. (1994). Thermal unfolding of tetrameric melittin: Comparison with the molten globule state of cytochrome c. Protein Sci. 3, 1418-1429.
    • (1994) Protein Sci. , vol.3 , pp. 1418-1429
    • Hagihara, Y.1    Oobatake, M.2    Goto, Y.3
  • 61
    • 0025195499 scopus 로고
    • Mechanism of acid-induced folding of proteins
    • Goto, Y., Takahashi, N. & Fink, A. L. (1990). Mechanism of acid-induced folding of proteins. Biochemistry, 29, 3480-3488.
    • (1990) Biochemistry , vol.29 , pp. 3480-3488
    • Goto, Y.1    Takahashi, N.2    Fink, A.L.3
  • 62
    • 0035916258 scopus 로고    scopus 로고
    • Effect of salts on the stability and folding of staphylococcal nuclease
    • Nishimura, C., Uversky, V. N. & Fink, A. L. (2001). Effect of salts on the stability and folding of staphylococcal nuclease. Biochemistry, 40, 2113-2128.
    • (2001) Biochemistry , vol.40 , pp. 2113-2128
    • Nishimura, C.1    Uversky, V.N.2    Fink, A.L.3
  • 63
    • 0026351184 scopus 로고
    • Role of electrostatic repulsion in the acidic molten globule of cytochrome c
    • Goto, Y. & Nishikori, S. (1991). Role of electrostatic repulsion in the acidic molten globule of cytochrome c. J. Mol. Biol. 222, 679-686.
    • (1991) J. Mol. Biol. , vol.222 , pp. 679-686
    • Goto, Y.1    Nishikori, S.2
  • 64
    • 0032568639 scopus 로고    scopus 로고
    • Alternative models for describing the acid unfolding of the apomyoglobin folding intermediate
    • Kay, M. S. & 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
  • 65
    • 0029598779 scopus 로고
    • Folding pathway of Escherichia coli ribonuclease HI: A circular dichroism, fluorescence, and NMR study
    • Yamasaki, K., Ogasahara, K., Yutani, Y., Oobatake, M. & Kanaya, S. (1995). Folding pathway of Escherichia coli ribonuclease HI: A circular dichroism, fluorescence, and NMR study. Biochemistry, 34, 16552-16561.
    • (1995) Biochemistry , vol.34 , pp. 16552-16561
    • Yamasaki, K.1    Ogasahara, K.2    Yutani, Y.3    Oobatake, M.4    Kanaya, S.5
  • 66
    • 0030961780 scopus 로고    scopus 로고
    • The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
    • Raschke, T. M. & Marqusee, S. (1997). The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Struct. Biol. 4, 298-304.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 298-304
    • Raschke, T.M.1    Marqusee, S.2
  • 67
    • 0033550298 scopus 로고    scopus 로고
    • The cooperativity of burst phase reactions explored
    • Parker, M. J. & Marqusee, S. (1999). The cooperativity of burst phase reactions explored. J. Mol. Biol. 293, 1195-1210.
    • (1999) J. Mol. Biol. , vol.293 , pp. 1195-1210
    • Parker, M.J.1    Marqusee, S.2
  • 69
    • 0028053016 scopus 로고
    • Equilibrium unfolding studies of barstar: Evidence for an alternative conformation which resembles a molten globule
    • Khurana, R. & Udgaonkar, J. B. (1994). Equilibrium unfolding studies of barstar: Evidence for an alternative conformation which resembles a molten globule. Biochemistry, 33, 106-115.
    • (1994) Biochemistry , vol.33 , pp. 106-115
    • Khurana, R.1    Udgaonkar, J.B.2
  • 70
    • 0001417468 scopus 로고
    • Action de l'acide carbonique sur les solutions dessels a acides forts. Etude absortiometrique
    • Setschenow, M. (1892). Action de l'acide carbonique sur les solutions dessels a acides forts. Etude absortiometrique. Ann. Chim. Phys. 25, 226-270.
    • (1892) Ann. Chim. Phys. , vol.25 , pp. 226-270
    • Setschenow, M.1
  • 72
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. (1998). Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated. Advan. Protein Chem. 51, 355-432.
    • (1998) Advan. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 73
    • 0000144150 scopus 로고
    • Salt dependence of oligoion polyion binding - A thermodynamic description based on preferential interaction coefficients
    • Anderson, C. F. & Record, M. T., Jr (1993). Salt dependence of oligoion polyion binding - A thermodynamic description based on preferential interaction coefficients. J. Phys. Chem. 97, 7116-7126.
    • (1993) J. Phys. Chem. , vol.97 , pp. 7116-7126
    • Anderson, C.F.1    Record M.T., Jr.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.