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Volumn 289, Issue 1, 1999, Pages 187-193

Thermodynamics of the unfolding of the cold-shock protein from Thermotoga maritima

Author keywords

Cold shock protein; Differential scanning calorimetry (DSC); Hyperthermophiles; Stability; Thermotoga maritima

Indexed keywords

COLD SHOCK PROTEIN; NUCLEIC ACID;

EID: 0033612222     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.2772     Document Type: Article
Times cited : (63)

References (37)
  • 1
    • 0026764471 scopus 로고
    • Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: Why small proteins tend to have high denaturation temperatures
    • Alexander P., Fahnestock S., Lee T., Orban J., Bryan P. Thermodynamic analysis of the folding of the streptococcal protein G IgG-binding domains B1 and B2: why small proteins tend to have high denaturation temperatures. Biochemistry. 31:1992;3597-3603.
    • (1992) Biochemistry , vol.31 , pp. 3597-3603
    • Alexander, P.1    Fahnestock, S.2    Lee, T.3    Orban, J.4    Bryan, P.5
  • 2
    • 0028978967 scopus 로고
    • Thermodynamics of the thermal unfolding of eglin c in the presence and absence of guanidinium chloride
    • Bae S.-J., Sturtevant J. M. Thermodynamics of the thermal unfolding of eglin c in the presence and absence of guanidinium chloride. Biophys. Chem. 55:1995;247-252.
    • (1995) Biophys. Chem. , vol.55 , pp. 247-252
    • Bae, S.-J.1    Sturtevant, J.M.2
  • 3
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin R. L. Temperature dependence of the hydrophobic interaction in protein folding. Proc. Natl Acad. Sci. USA. 83:1986;8069-8072.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 4
    • 0031658803 scopus 로고    scopus 로고
    • A superfamily of proteins that contain the cold-shock domain
    • Graumann P. L., Marahiel M. A. A superfamily of proteins that contain the cold-shock domain. Trends Biochem. Sci. 23:1998;286-290.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 286-290
    • Graumann, P.L.1    Marahiel, M.A.2
  • 6
    • 0019555878 scopus 로고
    • Nuclear magnetic resonance study on the microenvironments of histidine residues of ribonuclease T1 and carboxymethylated ribonuclease T1
    • Inagaki F., Kawano Y., Shimada I., Takahashi K., Miyazawa T. Nuclear magnetic resonance study on the microenvironments of histidine residues of ribonuclease T1 and carboxymethylated ribonuclease T1. J. Biochem. Tokyo. 89:1981;1185-1195.
    • (1981) J. Biochem. Tokyo , vol.89 , pp. 1185-1195
    • Inagaki, F.1    Kawano, Y.2    Shimada, I.3    Takahashi, K.4    Miyazawa, T.5
  • 8
    • 0026320508 scopus 로고
    • Protein stability and molecular adaptation to extreme conditions
    • Jaenicke R. Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202:1991;715-728.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 715-728
    • Jaenicke, R.1
  • 9
    • 0032011351 scopus 로고    scopus 로고
    • What ultrastable proteins teach us about protein stability
    • Jaenicke R. What ultrastable proteins teach us about protein stability. Biochemistry (Moscow). 63:1998;312-321.
    • (1998) Biochemistry (Moscow) , vol.63 , pp. 312-321
    • Jaenicke, R.1
  • 10
    • 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., Ladenstein R. Thermal unfolding of the DNA-binding protein Sso7d from the hyperthermophile Sulfolobus solfataricus. J. Mol. Biol. 264:1996;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
  • 11
    • 0002527319 scopus 로고    scopus 로고
    • Thermodynamic background to differential scanning calorimetry
    • J. E. Ladbury, & B. Z. Chowdhry. Chichester: John Wiley & Sons
    • Leharne S. A., Chowdhry B. Z. Thermodynamic background to differential scanning calorimetry. Ladbury J. E., Chowdhry B. Z. Biocalorimetry: Applications of Calorimetry in the Biological Sciences. 1998;157-182 John Wiley & Sons, Chichester.
    • (1998) Biocalorimetry: Applications of Calorimetry in the Biological Sciences , pp. 157-182
    • Leharne, S.A.1    Chowdhry, B.Z.2
  • 12
    • 0029917969 scopus 로고    scopus 로고
    • The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding
    • Liu Y., Sturtevant J. M. The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding. Biochemistry. 35:1996;3059-3062.
    • (1996) Biochemistry , vol.35 , pp. 3059-3062
    • Liu, Y.1    Sturtevant, J.M.2
  • 13
    • 0025906146 scopus 로고
    • Contribution of the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area
    • Livingstone J. R., Spolar R. S., Record M. T. Jr. Contribution of the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface area. Biochemistry. 30:1991;4237-4244.
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.R.1    Spolar, R.S.2    Record M.T., Jr.3
  • 14
    • 0028593677 scopus 로고
    • Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis
    • Makhatadze G. I., Marahiel M. A. Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis. Protein Sci. 3:1994;2144-2147.
    • (1994) Protein Sci. , vol.3 , pp. 2144-2147
    • Makhatadze, G.I.1    Marahiel, M.A.2
  • 15
    • 0030582620 scopus 로고    scopus 로고
    • Hyperthermophile protein folding thermodynamics: Differential scanning calorimetry and chemical denaturation of Sac7d
    • McCrary B. S., Bedell J., Edmondson S. P., Shriver J. W. Hyperthermophile protein folding thermodynamics: differential scanning calorimetry and chemical denaturation of Sac7d. J. Mol. Biol. 264:1996;784-805.
    • (1996) J. Mol. Biol. , vol.264 , pp. 784-805
    • McCrary, B.S.1    Bedell, J.2    Edmondson, S.P.3    Shriver, J.W.4
  • 16
    • 0032512877 scopus 로고    scopus 로고
    • Linkage of protonation and anion binding to the folding of Sac7d
    • McCrary B. S., Bedell J., Edmondson S. P., Shriver J. W. Linkage of protonation and anion binding to the folding of Sac7d. J. Mol. Biol. 276:1998;203-224.
    • (1998) J. Mol. Biol. , vol.276 , pp. 203-224
    • McCrary, B.S.1    Bedell, J.2    Edmondson, S.P.3    Shriver, J.W.4
  • 17
    • 0025044680 scopus 로고
    • Contribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58→Ala
    • McNutt M., Mullins L. S., Raushel F. M., Pace C. N. Contribution of histidine residues to the conformational stability of ribonuclease T1 and mutant Glu-58→Ala. Biochemistry. 29:1990;7572-7576.
    • (1990) Biochemistry , vol.29 , pp. 7572-7576
    • McNutt, M.1    Mullins, L.S.2    Raushel, F.M.3    Pace, C.N.4
  • 18
    • 0026756702 scopus 로고
    • Thermodynamics of structural stability and cooperative folding behaviour in proteins
    • Murphy K. P., Freire E. Thermodynamics of structural stability and cooperative folding behaviour in proteins. Advan. Protein Chem. 43:1992;313-361.
    • (1992) Advan. Protein Chem. , vol.43 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 19
    • 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., Scholtz J. M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4:1995;2138-2148.
    • (1995) Protein Sci. , vol.4 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 20
    • 0028234777 scopus 로고
    • Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: Identification of a binding epitope for DNA
    • Newkirk K., Feng W., Jiang W., Tejero R., Emerson S. D., Inouye M., Montelione G. T. Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA. Proc. Natl Acad. Sci. USA. 91:1994;5114-5118.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5114-5118
    • Newkirk, K.1    Feng, W.2    Jiang, W.3    Tejero, R.4    Emerson, S.D.5    Inouye, M.6    Montelione, G.T.7
  • 21
    • 0025271463 scopus 로고
    • PH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1
    • Pace C. N., Laurents D. V., Thomson J. A. pH dependence of the urea and guanidine hydrochloride denaturation of ribonuclease A and ribonuclease T1. Biochemistry. 29:1990;2564-2572.
    • (1990) Biochemistry , vol.29 , pp. 2564-2572
    • Pace, C.N.1    Laurents, D.V.2    Thomson, J.A.3
  • 24
    • 0024199422 scopus 로고
    • Stability of protein structure and hydrophobic interaction
    • Privalov P. L., Gill S. J. Stability of protein structure and hydrophobic interaction. Advan. Protein Chem. 39:1988;191-234.
    • (1988) Advan. Protein Chem. , vol.39 , pp. 191-234
    • Privalov, P.L.1    Gill, S.J.2
  • 25
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure
    • Privalov P. L., Khechinashvili N. N. A thermodynamic approach to the problem of stabilization of globular protein structure. J. Mol. Biol. 86:1974;665-684.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 27
    • 0027296211 scopus 로고
    • Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein
    • Schindelin H., Marahiel M. A., Heinemann U. Universal nucleic acid-binding domain revealed by crystal structure of the B. subtilis major cold-shock protein. Nature. 364:1993;164-168.
    • (1993) Nature , vol.364 , pp. 164-168
    • Schindelin, H.1    Marahiel, M.A.2    Heinemann, U.3
  • 30
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant J. M. Heat capacity and entropy changes in processes involving proteins. Proc. Natl Acad. Sci. USA. 74:1977;2236-2240.
    • (1977) Proc. Natl Acad. Sci. USA , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 31
    • 77956727554 scopus 로고
    • The interpretation of hydrogen ion titration curves of proteins
    • Tanford C. The interpretation of hydrogen ion titration curves of proteins. Advan. Protein Chem. 17:1962;69-165.
    • (1962) Advan. Protein Chem. , vol.17 , pp. 69-165
    • Tanford, C.1
  • 35
    • 0344334040 scopus 로고    scopus 로고
    • Cloning, overexpression, purification and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotogamaritima
    • Welker C., Böhm G., Schurig H., Jaenicke R. Cloning, overexpression, purification and physicochemical characterization of a cold shock protein homolog from the hyperthermophilic bacterium Thermotogamaritima. Protein Sci. 8:1999;394-403.
    • (1999) Protein Sci. , vol.8 , pp. 394-403
    • Welker, C.1    Böhm, G.2    Schurig, H.3    Jaenicke, R.4


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