메뉴 건너뛰기




Volumn 42, Issue 17, 2003, Pages 4864-4873

Temperature range of thermodynamic stability for the native state of reversible two-state proteins

Author keywords

[No Author keywords available]

Indexed keywords

COMPUTER SIMULATION; CORRELATION METHODS; HYDROPHOBICITY; SPECIFIC HEAT; THERMODYNAMIC STABILITY;

EID: 0038333434     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi027184+     Document Type: Article
Times cited : (39)

References (54)
  • 1
    • 0023442217 scopus 로고
    • Protein stability curves
    • Becktel, W., and Schellman, J. A. (1987) Protein stability curves, Biopolymers 26, 1859-1877.
    • (1987) Biopolymers , vol.26 , pp. 1859-1877
    • Becktel, W.1    Schellman, J.A.2
  • 3
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann, W. (1959) Some factors in the interpretation of protein denaturation, Adv. Protein Chem. 14, 1-63.
    • (1959) Adv. Protein Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 4
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill, K. A. (1990) Dominant forces in protein folding, Biochemistry 29, 7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 5
    • 0030834850 scopus 로고    scopus 로고
    • Temperature, stability and hydrophobic interaction
    • Schellman, J. A. (1997) Temperature, stability and hydrophobic interaction, Biophys. J. 73, 2960-2964.
    • (1997) Biophys. J. , vol.73 , pp. 2960-2964
    • Schellman, J.A.1
  • 6
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace, C. N., Shirley, B. A., McNutt, M., and Gajiwala, K. (1996) Forces contributing to the conformational stability of proteins, FASEB J. 10, 75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 8
    • 0035895356 scopus 로고    scopus 로고
    • Polar group burial contributes more to protein stability than nonpolar group burial
    • Pace, C. N. (2001) Polar Group Burial Contributes More to Protein Stability than Nonpolar Group Burial, Biochemistry 40, 310-313.
    • (2001) Biochemistry , vol.40 , pp. 310-313
    • Pace, C.N.1
  • 9
    • 0037197677 scopus 로고    scopus 로고
    • Maximal stabilities of reversible two-state proteins
    • Kumar, S., Tsai, C. J., and Nussinov, R. (2002) Maximal stabilities of reversible two-state proteins, Biochemistry 41, 5359-5374.
    • (2002) Biochemistry , vol.41 , pp. 5359-5374
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 10
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov, P. L., and Gill, S. J. (1988) Stability of protein structure and hydrophobic interaction, Adv. Protein Chem. 39, 191-234.
    • (1988) Adv. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 11
    • 0033538553 scopus 로고    scopus 로고
    • Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability
    • Thomson, M. J., and Eisenberg, D. (1999) Transproteomic evidence of a loop-deletion mechanism for enhancing protein thermostability, J. Mol. Biol. 290, 595-604.
    • (1999) J. Mol. Biol. , vol.290 , pp. 595-604
    • Thomson, M.J.1    Eisenberg, D.2
  • 12
    • 0030596013 scopus 로고    scopus 로고
    • Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus
    • Knapp, S., Karshikoff, A., Berndt, K. D., Christova, P., Atanasov, B., and Ladenstein, R. (1996) Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus, J. Mol. Biol. 264, 1132-1144.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1132-1144
    • Knapp, S.1    Karshikoff, A.2    Berndt, K.D.3    Christova, P.4    Atanasov, B.5    Ladenstein, R.6
  • 13
    • 0033612222 scopus 로고    scopus 로고
    • Thermodynamics of the unfolding of the cold shock protein from Thermotoga maritima
    • Wassenberg, D., Welker, C., and Jaenicke, R. (1999) Thermodynamics of the unfolding of the cold shock protein from Thermotoga maritima, J. Mol. Biol. 289, 187-193.
    • (1999) J. Mol. Biol. , vol.289 , pp. 187-193
    • Wassenberg, D.1    Welker, C.2    Jaenicke, R.3
  • 15
    • 0028966932 scopus 로고
    • Conformational stability of HPr: The histidine-containing phosphocarrier protein from Bacillus subtilis
    • Scholtz, J. M. (1995) Conformational stability of HPr: The histidine-containing phosphocarrier protein from Bacillus subtilis, Protein Sci 4, 35-43.
    • (1995) Protein Sci. , vol.4 , pp. 35-43
    • Scholtz, J.M.1
  • 16
    • 0029934661 scopus 로고    scopus 로고
    • Heat and cold denatured states of monomeric λ repressor are thermodynamically and chemically equivalent
    • Huang, G. S., and Oas, T. G. (1996) Heat and cold denatured states of monomeric λ repressor are thermodynamically and chemically equivalent, Biochemistry 35, 6173-6180.
    • (1996) Biochemistry , vol.35 , pp. 6173-6180
    • Huang, G.S.1    Oas, T.G.2
  • 18
    • 0024298839 scopus 로고
    • Stability mutants of staphylococcal nuclease: Large compensating enthalpyentropy changes for the reversible denaturation reaction
    • Shortle, D., Meeker, A. K., and Freire, E. (1988) Stability mutants of staphylococcal nuclease: Large compensating enthalpyentropy changes for the reversible denaturation reaction, Biochemistry 27, 4761-4768.
    • (1988) Biochemistry , vol.27 , pp. 4761-4768
    • Shortle, D.1    Meeker, A.K.2    Freire, E.3
  • 20
    • 0033858185 scopus 로고    scopus 로고
    • Thermal unfolding and conformational stability of recombinant domain II of glutamate dehydrogenase from the hyperthermophile Thermotoga maritima
    • Consalvi, V., Chiaraluce, R., Giangiacomo, L., Sandurra, R., Christova, P., Karshikoff, A., Knapp, S., and Ladenstein, R. (2000). Thermal unfolding and conformational stability of recombinant domain II of glutamate dehydrogenase from the hyperthermophile Thermotoga maritima, Protein Eng. 13, 501-507.
    • (2000) Protein Eng. , vol.13 , pp. 501-507
    • Consalvi, V.1    Chiaraluce, R.2    Giangiacomo, L.3    Sandurra, R.4    Christova, P.5    Karshikoff, A.6    Knapp, S.7    Ladenstein, R.8
  • 21
    • 0024993265 scopus 로고
    • Chemical modification of tryptophan residues and stability changes in proteins
    • Okajima, T., Kawata, Y., and Hamaguchi, K. (1990) Chemical modification of tryptophan residues and stability changes in proteins, Biochemistry 29, 9168-9175.
    • (1990) Biochemistry , vol.29 , pp. 9168-9175
    • Okajima, T.1    Kawata, Y.2    Hamaguchi, K.3
  • 22
    • 0001069985 scopus 로고
    • Calorimetric study of the thermal unfolding of Kunitz-type soybean trypsin inhibitor at pH 7.0
    • Fukada, H., Kitamura, S., and Takahashi, K. (1995) Calorimetric study of the thermal unfolding of Kunitz-type soybean trypsin inhibitor at pH 7.0, Thermochim. Acta 266, 365-372.
    • (1995) Thermochim. Acta , vol.266 , pp. 365-372
    • Fukada, H.1    Kitamura, S.2    Takahashi, K.3
  • 24
    • 0026754044 scopus 로고
    • A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range
    • Santoro, M. M., and Bolen, D. W. (1992) A test of the linear extrapolation of unfolding free energy changes over an extended denaturant concentration range, Biochemistry 31, 4901-4907.
    • (1992) Biochemistry , vol.31 , pp. 4901-4907
    • Santoro, M.M.1    Bolen, D.W.2
  • 25
    • 0028788480 scopus 로고
    • Evidence for a two state transition in the folding process of the activation domain of human procarboxypeptidase A2
    • Villegas, V., Azuaga, A., Catasus, L., Reverter, D., Mateo, P. L., Avilles, F. X., and Serrano, L. (1995) Evidence for a two state transition in the folding process of the activation domain of human procarboxypeptidase A2, Biochemistry 34, 15105-15110.
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1    Azuaga, A.2    Catasus, L.3    Reverter, D.4    Mateo, P.L.5    Avilles, F.X.6    Serrano, L.7
  • 26
    • 0030582620 scopus 로고    scopus 로고
    • Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d
    • McCrary, B. S., Edmondson, S. P., and Shriver, J. W. (1996) Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d, J. Mol. Biol. 264, 784-805.
    • (1996) J. Mol. Biol. , vol.264 , pp. 784-805
    • McCrary, B.S.1    Edmondson, S.P.2    Shriver, J.W.3
  • 28
    • 0029761976 scopus 로고    scopus 로고
    • Conformational stability of Escherichia coli HPr protein: Test of the linear extrapolation method and a thermodynamic characterization of cold denaturation
    • Nicholson, E. M., and Scholtz, J. M. (1996) Conformational stability of Escherichia coli HPr protein: Test of the linear extrapolation method and a thermodynamic characterization of cold denaturation, Biochemistry 35, 11369-11378.
    • (1996) Biochemistry , vol.35 , pp. 11369-11378
    • Nicholson, E.M.1    Scholtz, J.M.2
  • 30
    • 0031012563 scopus 로고    scopus 로고
    • Hydrophobic folding units derived from dissimilar monomer structures and their interactions
    • Tsai, C. J., and Nussinov, R. (1997) Hydrophobic folding units derived from dissimilar monomer structures and their interactions, Protein Sci. 6, 24-42.
    • (1997) Protein Sci. , vol.6 , pp. 24-42
    • Tsai, C.J.1    Nussinov, R.2
  • 31
    • 0030756203 scopus 로고    scopus 로고
    • Hydrophobic folding units at protein-protein interfaces: Implications to protein folding and protein-protein association
    • Tsai, C. J., and Nussinov, R. (1997) Hydrophobic folding units at protein-protein interfaces: Implications to protein folding and protein-protein association, Protein Sci. 6, 1426-1437.
    • (1997) Protein Sci. , vol.6 , pp. 1426-1437
    • Tsai, C.J.1    Nussinov, R.2
  • 32
    • 0029411262 scopus 로고
    • Occluded molecular surface: Analysis of protein packing
    • Pattabiraman, N., Ward, K. B., and Fleming, P. J. (1995) Occluded Molecular Surface: Analysis of Protein Packing, J. Mol. Recognit. 8, 334-344.
    • (1995) J. Mol. Recognit. , vol.8 , pp. 334-344
    • Pattabiraman, N.1    Ward, K.B.2    Fleming, P.J.3
  • 33
    • 0034595515 scopus 로고    scopus 로고
    • Protein packing: Dependence on protein size, secondary structure and amino acid composition
    • Fleming, P. J., and Richards, F. M. (2000) Protein Packing: Dependence on Protein Size, Secondary Structure and Amino Acid Composition, J. Mol. Biol. 299, 487-498.
    • (2000) J. Mol. Biol. , vol.299 , pp. 487-498
    • Fleming, P.J.1    Richards, F.M.2
  • 35
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S., Tsai, C. J., and Nussinov, R. (2000) Factors enhancing protein thermostability, Protein Eng. 13, 179-191.
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 37
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers, J. K., Pace, C. N., and Scholtz, J. M. (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
  • 38
    • 0033975702 scopus 로고    scopus 로고
    • Structural energetics of protein folding and binding
    • Edgcomb, S. P., and Murphy, K. P. (2000) Structural energetics of protein folding and binding, Curr. Opin. Biotechnol. 11, 62-66.
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 62-66
    • Edgcomb, S.P.1    Murphy, K.P.2
  • 39
    • 0033753811 scopus 로고    scopus 로고
    • Domain size distributions can predict domain boundaries
    • Wheelan, S. J., Marchler-Bauer, A., and Bryant, S. H. (2000) Domain size distributions can predict domain boundaries, Bio-informatics 16, 613-618.
    • (2000) Bioinformatics , vol.16 , pp. 613-618
    • Wheelan, S.J.1    Marchler-Bauer, A.2    Bryant, S.H.3
  • 40
    • 0035865948 scopus 로고    scopus 로고
    • Protein structural domains: Analysis of the 3Dee domains database
    • Dengler, U., Siddiqui, A. S., and Barton, G. J. (2001) Protein structural domains: Analysis of the 3Dee domains database, Proteins 42, 332-344.
    • (2001) Proteins , vol.42 , pp. 332-344
    • Dengler, U.1    Siddiqui, A.S.2    Barton, G.J.3
  • 41
    • 0031932170 scopus 로고    scopus 로고
    • Favorable domain size in proteins
    • Xu, D., and Nussinov, R. (1998) Favorable domain size in proteins, Folding Des. 3, 11-17.
    • (1998) Folding Des. , vol.3 , pp. 11-17
    • Xu, D.1    Nussinov, R.2
  • 42
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the Streptococcal protein IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures
    • Alexander, P., Fahnestock, S., Lee, T., Orban, J., and Bryan, P. (1992) Thermodynamic analysis of the folding of the Streptococcal protein IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures, Biochemistry 31, 3597-3603.
    • (1992) Biochemistry , vol.31 , pp. 3597-3603
    • Alexander, P.1    Fahnestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 43
    • 0030822593 scopus 로고    scopus 로고
    • Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 °C
    • Hiller, R., Zhou, Z. H., Adams, M. W., and Englander, S. W. (1997) Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200 °C, Proc. Natl. Acad. Sci. U.S.A. 94, 11329-11332.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 11329-11332
    • Hiller, R.1    Zhou, Z.H.2    Adams, M.W.3    Englander, S.W.4
  • 44
    • 0029644328 scopus 로고
    • Hyperthermophiles: Taking the heat and loving it
    • Rees, D. C., and Adams, M. W. W. (1995) Hyperthermophiles: Taking the heat and loving it, Structure 3, 251-254.
    • (1995) Structure , vol.3 , pp. 251-254
    • Rees, D.C.1    Adams, M.W.W.2
  • 45
    • 0033596744 scopus 로고    scopus 로고
    • Comparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme
    • Beadle, B. M., Baase, W. A., Wilson, D. B., Gilkes, N. R., and Shoichet, B. K. (1999) Comparing the thermodynamic stabilities of a related thermophilic and mesophilic enzyme, Biochemistry 38, 2570-2576.
    • (1999) Biochemistry , vol.38 , pp. 2570-2576
    • Beadle, B.M.1    Baase, W.A.2    Wilson, D.B.3    Gilkes, N.R.4    Shoichet, B.K.5
  • 46
    • 0035000257 scopus 로고    scopus 로고
    • Some thermodynamic implications for the thermostability of proteins
    • Rees, D. C., and Robertson, A. D. (2001) Some thermodynamic implications for the thermostability of proteins, Protein Sci. 10, 1187-1194.
    • (2001) Protein Sci. , vol.10 , pp. 1187-1194
    • Rees, D.C.1    Robertson, A.D.2
  • 47
    • 0035960641 scopus 로고    scopus 로고
    • Thermodynamic differences among homologous thermophilic and mesophilic proteins
    • Kumar, S., Tsai, C. J., and Nussinov, R. (2001) Thermodynamic differences among homologous thermophilic and mesophilic proteins, Biochemistry 40, 14152-14165.
    • (2001) Biochemistry , vol.40 , pp. 14152-14165
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 48
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle, D., and Ackerman, M. S. (2001) Persistence of native-like topology in a denatured protein in 8 M urea, Science 293, 487-489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 49
    • 0000159569 scopus 로고    scopus 로고
    • Protein structure and energetics of protein stability
    • Robertson, A. D., and Murphy, K. P. (1997) Protein structure and energetics of protein stability, Chem. Rev. 97, 1251-1267.
    • (1997) Chem. Rev. , vol.97 , pp. 1251-1267
    • Robertson, A.D.1    Murphy, K.P.2
  • 50
    • 0036252440 scopus 로고    scopus 로고
    • The hydrophobic effect: A new insight from cold denaturation and a two state water structure
    • Tsai, C. J., Maizel, J. V., Jr., and Nussinov, R. (2002) The hydrophobic effect: A new insight from cold denaturation and a two state water structure, Crit. Rev. Biochem. Mol. Biol. 37, 55-69.
    • (2002) Crit. Rev. Biochem. Mol. Biol. , vol.37 , pp. 55-69
    • Tsai, C.J.1    Maizel J.V., Jr.2    Nussinov, R.3
  • 51
    • 0033550299 scopus 로고    scopus 로고
    • Salt bridge stability in monomeric proteins
    • Kumar, S., and Nussinov, R. (1999) Salt bridge stability in monomeric proteins, J. Mol. Biol. 293, 1241-1255.
    • (1999) J. Mol. Biol. , vol.293 , pp. 1241-1255
    • Kumar, S.1    Nussinov, R.2
  • 52
    • 0033994586 scopus 로고    scopus 로고
    • Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers
    • Kumar, S., Ma, B., Tsai, C. J., and Nussinov, R. (2000) Electrostatic strengths of salt bridges in thermophilic and mesophilic glutamate dehydrogenase monomers, Proteins 38, 368-383.
    • (2000) Proteins , vol.38 , pp. 368-383
    • Kumar, S.1    Ma, B.2    Tsai, C.J.3    Nussinov, R.4
  • 53
    • 0034495733 scopus 로고    scopus 로고
    • Aromatic clusters: A determinant of thermal stability of thermophilic proteins
    • Kannan, N., and Vishveshwara, S. (2000) Aromatic clusters: a determinant of thermal stability of thermophilic proteins, Protein Eng. 13, 753-761.
    • (2000) Protein Eng. , vol.13 , pp. 753-761
    • Kannan, N.1    Vishveshwara, S.2
  • 54
    • 0037172796 scopus 로고    scopus 로고
    • Elucidation of factors responsible for enhanced thermal stability of proteins: A structural genomics based study
    • Chakravarty, S., and Varadarajan, R. (2002) Elucidation of factors responsible for enhanced thermal stability of proteins: A structural genomics based study, Biochemistry 41, 8152-8161.
    • (2002) Biochemistry , vol.41 , pp. 8152-8161
    • Chakravarty, S.1    Varadarajan, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.