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Volumn 91, Issue 8, 2006, Pages 2826-2832

Long-lived conformational isomerism of protein dimers: The role of the free energy of subunit association

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; OLIGOMER; PROTEIN SUBUNIT; TRIOSEPHOSPHATE ISOMERASE;

EID: 33749518052     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.089706     Document Type: Article
Times cited : (6)

References (31)
  • 1
  • 2
    • 0025845307 scopus 로고
    • Oligomeric protein associations: Transition from stochastic to deterministic equilibrium
    • Erijman, L., and G. Weber. 1991. Oligomeric protein associations: transition from stochastic to deterministic equilibrium. Biochemistry. 30:1595-1599.
    • (1991) Biochemistry , vol.30 , pp. 1595-1599
    • Erijman, L.1    Weber, G.2
  • 3
    • 0029954416 scopus 로고    scopus 로고
    • Deterministic pressure dissociation and unfolding of triose phosphate isomerase: Persistent heterogeneity of a protein dimer
    • Rietveld, A. W. M., and S. T. Ferreira. 1996. Deterministic pressure dissociation and unfolding of triose phosphate isomerase: persistent heterogeneity of a protein dimer. Biochemistry. 35:7743-7751.
    • (1996) Biochemistry , vol.35 , pp. 7743-7751
    • Rietveld, A.W.M.1    Ferreira, S.T.2
  • 4
    • 0032548449 scopus 로고    scopus 로고
    • Kinetics and energetics of subunit dissociation/unfolding of TIM: The importance of oligomerization for conformational persistence and chemical stability of proteins
    • Rietveld, A. W. M., and S. T. Ferreira. 1998. Kinetics and energetics of subunit dissociation/unfolding of TIM: the importance of oligomerization for conformational persistence and chemical stability of proteins. Biochemistry. 37:933-937.
    • (1998) Biochemistry , vol.37 , pp. 933-937
    • Rietveld, A.W.M.1    Ferreira, S.T.2
  • 5
    • 0346365102 scopus 로고    scopus 로고
    • Persistent conformational heterogeneity of triosephosphate isomerase: Separation and characterization of conformational isomers in solution
    • Moreau, V. H., A. W. Rietveld, and S. T. Ferreira. 2003. Persistent conformational heterogeneity of triosephosphate isomerase: separation and characterization of conformational isomers in solution. Biochemistry. 42:14831-14837.
    • (2003) Biochemistry , vol.42 , pp. 14831-14837
    • Moreau, V.H.1    Rietveld, A.W.2    Ferreira, S.T.3
  • 6
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C. N. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 7
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., C. N. Pace, and J. M. Scholtz. 1995. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 8
    • 0028349918 scopus 로고
    • Deterministic pressure-induced dissociation of vicilin, the 7S storage globulin from pea seeds: Effects of pH and cosolvents on oligomer stability
    • Pedrosa, C., and S. T. Ferreira. 1994. Deterministic pressure-induced dissociation of vicilin, the 7S storage globulin from pea seeds: effects of pH and cosolvents on oligomer stability. Biochemistry. 33:4046-4055.
    • (1994) Biochemistry , vol.33 , pp. 4046-4055
    • Pedrosa, C.1    Ferreira, S.T.2
  • 9
    • 0024278087 scopus 로고
    • Pressure-induced dissociation of brome mosaic virus
    • Silva, J. L., and G. Weber. 1988. Pressure-induced dissociation of brome mosaic virus. J. Mol. Biol. 199:149-159.
    • (1988) J. Mol. Biol. , vol.199 , pp. 149-159
    • Silva, J.L.1    Weber, G.2
  • 10
    • 0024431526 scopus 로고
    • Anomalous pressure dissociation of large protein aggregates. Lack of concentration dependence and irreversibility at extreme degrees of dissociation of extracellular hemoglobin
    • Silva, J. L., M. Villas-Boas, C. F. S. Bonafe, and N. C. Meirelles. 1989. Anomalous pressure dissociation of large protein aggregates. Lack of concentration dependence and irreversibility at extreme degrees of dissociation of extracellular hemoglobin. J. Biol. Chem. 264:15863-15868.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15863-15868
    • Silva, J.L.1    Villas-Boas, M.2    Bonafe, C.F.S.3    Meirelles, N.C.4
  • 11
    • 0025737960 scopus 로고
    • Reassembly of a large multisubunit protein promoted by nonprotein factors. Effects of calcium and glycerol on the association of extracellular hemoglobin
    • Bonafé, C. F. S., M. Villas-Boas, M. C. Suarez, and J. L. Silva. 1991. Reassembly of a large multisubunit protein promoted by nonprotein factors. Effects of calcium and glycerol on the association of extracellular hemoglobin. J. Biol. Chem. 266:13210-13216.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13210-13216
    • Bonafé, C.F.S.1    Villas-Boas, M.2    Suarez, M.C.3    Silva, J.L.4
  • 12
    • 0027268092 scopus 로고
    • Reversible pressure dissociation of R17 bacteriophage. The physical individuality of virus particles
    • Da Poian, A., L. P. Oliveira, J. L. Gaspar, J. L. Silva, and G. Weber. 1993. Reversible pressure dissociation of R17 bacteriophage. The physical individuality of virus particles. J. Mol. Biol. 231:999-1008.
    • (1993) J. Mol. Biol. , vol.231 , pp. 999-1008
    • Da Poian, A.1    Oliveira, L.P.2    Gaspar, J.L.3    Silva, J.L.4    Weber, G.5
  • 13
    • 0030031616 scopus 로고    scopus 로고
    • Concentration dependence of the subunit association of oligomers and viruses and the modification of the latter by urea binding
    • Weber, G., A. T. Da Poian, and J. L. Silva. 1996. Concentration dependence of the subunit association of oligomers and viruses and the modification of the latter by urea binding. Biophys. J. 70:167-173.
    • (1996) Biophys. J. , vol.70 , pp. 167-173
    • Weber, G.1    Da Poian, A.T.2    Silva, J.L.3
  • 14
    • 0019890116 scopus 로고
    • Pressure-induced reversible dissociation of enolase
    • Paladini, A. A., and G. Weber. 1981. Pressure-induced reversible dissociation of enolase. Biochemistry. 20:2587-2593.
    • (1981) Biochemistry , vol.20 , pp. 2587-2593
    • Paladini, A.A.1    Weber, G.2
  • 15
    • 0025748639 scopus 로고
    • Dissociation of purified erythrocyte Ca(21)-ATPase by hydrostatic pressure
    • Coelho-Sampaio, T., S. T. Ferreira, G. Benaim, and A. Vieyra. 1991. Dissociation of purified erythrocyte Ca(21)-ATPase by hydrostatic pressure. J. Biol. Chem. 266:22266-22272.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22266-22272
    • Coelho-Sampaio, T.1    Ferreira, S.T.2    Benaim, G.3    Vieyra, A.4
  • 16
    • 0026541905 scopus 로고
    • Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of arc repressor
    • Silva, J. L., C. F. Silveira, A. Correia, and L. Pontes. 1992. Dissociation of a native dimer to a molten globule monomer. Effects of pressure and dilution on the association equilibrium of arc repressor. J. Mol. Biol. 223:545-555.
    • (1992) J. Mol. Biol. , vol.223 , pp. 545-555
    • Silva, J.L.1    Silveira, C.F.2    Correia, A.3    Pontes, L.4
  • 17
    • 0023055734 scopus 로고
    • Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase
    • Silva, J. L., E. W. Miles, and G. Weber. 1986. Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase. Biochemistry. 25:5780-5786.
    • (1986) Biochemistry , vol.25 , pp. 5780-5786
    • Silva, J.L.1    Miles, E.W.2    Weber, G.3
  • 18
    • 0027258549 scopus 로고
    • Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase
    • Erijman, L., G. H. Lorimer, and G. Weber. 1993. Reversible dissociation and conformational stability of dimeric ribulose bisphosphate carboxylase. Biochemistry. 32:5187-5195.
    • (1993) Biochemistry , vol.32 , pp. 5187-5195
    • Erijman, L.1    Lorimer, G.H.2    Weber, G.3
  • 19
    • 0024276840 scopus 로고
    • Dissociation of yeast hexokinase by hydrostatic pressure
    • Ruan, K., and G. Weber. 1988. Dissociation of yeast hexokinase by hydrostatic pressure. Biochemistry. 27:3295-3301.
    • (1988) Biochemistry , vol.27 , pp. 3295-3301
    • Ruan, K.1    Weber, G.2
  • 20
  • 21
    • 0030031616 scopus 로고    scopus 로고
    • Concentration dependence of the subunit association of oligomers and viruses and the modification of the latter by urea binding
    • Weber, G., A. T. Da Poian, and J. L. Silva. 1996. Concentration dependence of the subunit association of oligomers and viruses and the modification of the latter by urea binding. Biophys. J. 70:167-173.
    • (1996) Biophys. J. , vol.70 , pp. 167-173
    • Weber, G.1    Da Poian, A.T.2    Silva, J.L.3
  • 22
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and H. J. Dyson. 1999. Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm. J. Mol. Biol. 293:321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 23
    • 0015819192 scopus 로고
    • Refolding of triose phosphate isomerase
    • Waley, S. G. 1973. Refolding of triose phosphate isomerase. Biochem. J. 135:165-172.
    • (1973) Biochem. J. , vol.135 , pp. 165-172
    • Waley, S.G.1
  • 24
    • 0026546576 scopus 로고
    • Relationship between the catalytic center and the primary degradation site of triosephosphate isomerase: Effects of active site modification and deamidation
    • Sun, A. Q., K. U. Yüksel, and R. W. Gracy. 1992. Relationship between the catalytic center and the primary degradation site of triosephosphate isomerase: effects of active site modification and deamidation. Arch. Biochem. Biophys. 293:382-390.
    • (1992) Arch. Biochem. Biophys. , vol.293 , pp. 382-390
    • Sun, A.Q.1    Yüksel, K.U.2    Gracy, R.W.3
  • 25
    • 0037444807 scopus 로고    scopus 로고
    • Thermodynamic characterization of yeast triosephosphate isomerase refolding: Insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme
    • Nájera, H., M. Costa, and D. A. Fernández-Velasco. 2003. Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme. Biochem. J. 370:785-792.
    • (2003) Biochem. J. , vol.370 , pp. 785-792
    • Nájera, H.1    Costa, M.2    Fernández-Velasco, D.A.3
  • 26
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere, P. A. 1987. Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56:89-124.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 27
    • 0344441463 scopus 로고    scopus 로고
    • Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: Evidence of conformational heterogeneity
    • Aparicio, R., S. T. Ferreira, and I. Polikarpov. 2003. Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. J. Mol. Biol. 334:1023-1041.
    • (2003) J. Mol. Biol. , vol.334 , pp. 1023-1041
    • Aparicio, R.1    Ferreira, S.T.2    Polikarpov, I.3
  • 31
    • 0035827364 scopus 로고    scopus 로고
    • PABMB lecture. Protein dynamics, folding and misfolding: From basic physical chemistry to human conformational diseases
    • Ferreira, S. T., and F. G. De Felice. 2001. PABMB lecture. Protein dynamics, folding and misfolding: from basic physical chemistry to human conformational diseases. FEBS Lett. 498:129-134.
    • (2001) FEBS Lett. , vol.498 , pp. 129-134
    • Ferreira, S.T.1    De Felice, F.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.