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Volumn 293, Issue 5, 1999, Pages 1241-1255

Salt bridge stability in monomeric proteins

Author keywords

Electrostatics; Geometry; Hierarchical folding; Salt bridge; Stability

Indexed keywords

MONOMER; PROTEIN;

EID: 0033550299     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3218     Document Type: Article
Times cited : (401)

References (45)
  • 1
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • Baldwin R. L., Rose G. D. Is protein folding hierarchic? II. Folding intermediates and transition states. Trends Biochem. Sci. 24:1999;77-84.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 77-84
    • Baldwin, R.L.1    Rose, G.D.2
  • 3
    • 84962348955 scopus 로고    scopus 로고
    • Salt bridge interactions: Stability of ionic and neutral complexes in the gas phase, in solution and in proteins
    • Barril X., Aleman C., Orozco M., Luque F. J. Salt bridge interactions: stability of ionic and neutral complexes in the gas phase, in solution and in proteins. Proteins: Struct. Funct. Genet. 32:1998;67-79.
    • (1998) Proteins: Struct. Funct. Genet. , vol.32 , pp. 67-79
    • Barril, X.1    Aleman, C.2    Orozco, M.3    Luque, F.J.4
  • 5
    • 0026345864 scopus 로고
    • Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme
    • Dao-pin S., Anderson D. E., Baase W. A., Dahlquist F. W., Matthews B. W. Structural and thermodynamic consequences of burying a charged residue within the hydrophobic core of T4 lysozyme. Biochemistry. 30:1991;11521-11529.
    • (1991) Biochemistry , vol.30 , pp. 11521-11529
    • Dao-Pin, S.1    Anderson, D.E.2    Baase, W.A.3    Dahlquist, F.W.4    Matthews, B.W.5
  • 6
    • 0344609869 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the hyperthermophilic protein Sac7d from Sulfolobus acidocaldarius: Contribution of salt bridges to thermostability
    • deBakker P. I. W., Hunenberger P. H., McCammon J. A. Molecular dynamics simulations of the hyperthermophilic protein Sac7d from Sulfolobus acidocaldarius: contribution of salt bridges to thermostability. J. Mol. Biol. 285:1999;1811-1830.
    • (1999) J. Mol. Biol. , vol.285 , pp. 1811-1830
    • Debakker, P.I.W.1    Hunenberger, P.H.2    McCammon, J.A.3
  • 7
    • 0032573431 scopus 로고    scopus 로고
    • The stability of salt bridges at high temperatures: Implications for hyperthermophilic proteins
    • Elcock A. H. The stability of salt bridges at high temperatures: implications for hyperthermophilic proteins. J. Mol. Biol. 284:1998;489-502.
    • (1998) J. Mol. Biol. , vol.284 , pp. 489-502
    • Elcock, A.H.1
  • 8
    • 0015505502 scopus 로고
    • Conformational equilibria in α- And δ- chymotrypsin. The energetics and importance of the salt bridge
    • Fersht A. R. Conformational equilibria in α- and δ- chymotrypsin. The energetics and importance of the salt bridge. J. Mol. Biol. 64:1972;497-509.
    • (1972) J. Mol. Biol. , vol.64 , pp. 497-509
    • Fersht, A.R.1
  • 9
    • 0023280069 scopus 로고
    • Calculation of electrostatic potential in an enzyme active site
    • Gilson M. K., Honig B. H. Calculation of electrostatic potential in an enzyme active site. Nature. 330:1987;84-86.
    • (1987) Nature , vol.330 , pp. 84-86
    • Gilson, M.K.1    Honig, B.H.2
  • 10
    • 0023779259 scopus 로고
    • Calculation of the total electrostatic energy of a macromolecular system: Solvation energies, binding energies, and conformational analysis
    • Gilson M. K., Honig B. H. Calculation of the total electrostatic energy of a macromolecular system: solvation energies, binding energies, and conformational analysis. Proteins: Struct. Funct. Genet. 4:1988;7-18.
    • (1988) Proteins: Struct. Funct. Genet. , vol.4 , pp. 7-18
    • Gilson, M.K.1    Honig, B.H.2
  • 11
    • 0021813940 scopus 로고
    • On the calculation of electrostatic interactions in proteins
    • Gilson M. K., Rashin A., Fine R., Honig B. On the calculation of electrostatic interactions in proteins. J. Mol. Biol. 183:1985;503-516.
    • (1985) J. Mol. Biol. , vol.183 , pp. 503-516
    • Gilson, M.K.1    Rashin, A.2    Fine, R.3    Honig, B.4
  • 12
    • 84988087911 scopus 로고
    • Calculating the electrostatic potential of molecules in solution: Method and error assessment
    • Gilson M. K., Sharp K. A., Honig B. H. Calculating the electrostatic potential of molecules in solution: method and error assessment. J. Comp. Chem. 9:1988;327-335.
    • (1988) J. Comp. Chem. , vol.9 , pp. 327-335
    • Gilson, M.K.1    Sharp, K.A.2    Honig, B.H.3
  • 13
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins? A continuum electrostatic analysis
    • Hendsch Z. S., Tidor B. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3:1994;211-226.
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 14
    • 0001348705 scopus 로고    scopus 로고
    • Parameter dependence in continuum electrostatic calculations: A study using protein salt bridges
    • Hendsch Z. S., Sindelar C. V., Tidor B. Parameter dependence in continuum electrostatic calculations: a study using protein salt bridges. J. Phys. Chem. ser. B. 102:1998;4404-4410.
    • (1998) J. Phys. Chem. Ser. B , vol.102 , pp. 4404-4410
    • Hendsch, Z.S.1    Sindelar, C.V.2    Tidor, B.3
  • 15
    • 0000176654 scopus 로고
    • Stability of "salt bridges" in membrane proteins
    • Honig B. H., Hubell W. L. Stability of "salt bridges" in membrane proteins. Proc. Natl Acad. Sci. USA. 81:1984;5412-5416.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 5412-5416
    • Honig, B.H.1    Hubell, W.L.2
  • 16
    • 0029016182 scopus 로고
    • Classical electrostatics in biology and chemistry
    • Honig B., Nicholls A. Classical electrostatics in biology and chemistry. Science. 268:1995;1144-1149.
    • (1995) Science , vol.268 , pp. 1144-1149
    • Honig, B.1    Nicholls, A.2
  • 17
    • 33751385054 scopus 로고
    • Macroscopic models of aqueous solutions: Biological and chemical applications
    • Honig B., Sharp K., Yang A. Macroscopic models of aqueous solutions: biological and chemical applications. J. Phys. Chem. 97:1993;1101-1109.
    • (1993) J. Phys. Chem. , vol.97 , pp. 1101-1109
    • Honig, B.1    Sharp, K.2    Yang, A.3
  • 18
    • 0026587310 scopus 로고
    • Co-operative interactions during protein folding
    • Horovitz A., Fersht A. R. Co-operative interactions during protein folding. J. Mol. Biol. 224:1992;733-740.
    • (1992) J. Mol. Biol. , vol.224 , pp. 733-740
    • Horovitz, A.1    Fersht, A.R.2
  • 19
    • 0031003188 scopus 로고    scopus 로고
    • Contribution of a salt bridge to the thermostability of DNA binding protein HU from Bacillus stearothermophilus determined by site directed mutagenesis
    • Kawamura S., Tanaka I., Kimura M. Contribution of a salt bridge to the thermostability of DNA binding protein HU from Bacillus stearothermophilus determined by site directed mutagenesis. J. Biochem. 121:1997;448-455.
    • (1997) J. Biochem. , vol.121 , pp. 448-455
    • Kawamura, S.1    Tanaka, I.2    Kimura, M.3
  • 20
    • 0022964504 scopus 로고
    • Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: Effects of ionic strength and amino acid modification
    • Klapper I., Hagstrom R., Fine R., Sharp K., Honig B. Focusing of electric fields in the active site of Cu-Zn superoxide dismutase: effects of ionic strength and amino acid modification. Proteins: Struct. Funct. Genet. 1:1986;47-59.
    • (1986) Proteins: Struct. Funct. Genet. , vol.1 , pp. 47-59
    • Klapper, I.1    Hagstrom, R.2    Fine, R.3    Sharp, K.4    Honig, B.5
  • 21
    • 0032101291 scopus 로고    scopus 로고
    • Dissecting α-helices: Position specific analysis of α-helices in globular proteins
    • Kumar S., Bansal M. Dissecting α-helices: position specific analysis of α-helices in globular proteins. Proteins: Struct. Funct. Genet. 31:1998;460-476.
    • (1998) Proteins: Struct. Funct. Genet. , vol.31 , pp. 460-476
    • Kumar, S.1    Bansal, M.2
  • 23
    • 0015222647 scopus 로고
    • The interpretation of protein structures. Estimation of static accessibility
    • Lee B. K., Richards F. M. The interpretation of protein structures. Estimation of static accessibility. J. Mol. Biol. 55:1971;379-400.
    • (1971) J. Mol. Biol. , vol.55 , pp. 379-400
    • Lee, B.K.1    Richards, F.M.2
  • 24
    • 0030917740 scopus 로고    scopus 로고
    • Exceptionally stable salt bridges in cytochrome P450cam have functional roles
    • Lounnas V., Wade R. C. Exceptionally stable salt bridges in cytochrome P450cam have functional roles. Biochemistry. 36:1997;5402-5417.
    • (1997) Biochemistry , vol.36 , pp. 5402-5417
    • Lounnas, V.1    Wade, R.C.2
  • 25
    • 0028574137 scopus 로고
    • Contribution of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structures in lambda repressor
    • Marqusee S., Sauer R. T. Contribution of a hydrogen bond/salt bridge network to the stability of secondary and tertiary structures in lambda repressor. Protein Sci. 3:1994;2217-2225.
    • (1994) Protein Sci. , vol.3 , pp. 2217-2225
    • Marqusee, S.1    Sauer, R.T.2
  • 26
    • 0029588555 scopus 로고
    • Complex salt bridges in proteins: Statistical analysis of structure and function
    • Musafia B., Buchner V., Arad D. Complex salt bridges in proteins: statistical analysis of structure and function. J. Mol. Biol. 254:1995;761-770.
    • (1995) J. Mol. Biol. , vol.254 , pp. 761-770
    • Musafia, B.1    Buchner, V.2    Arad, D.3
  • 27
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in haemoglobin
    • Perutz M. F. Stereochemistry of cooperative effects in haemoglobin. Nature. 228:1970;726-739.
    • (1970) Nature , vol.228 , pp. 726-739
    • Perutz, M.F.1
  • 28
    • 0030596082 scopus 로고    scopus 로고
    • Structural role of a buried salt bridge in the 434 repressor DNA-binding domain
    • Pervushin K., Billeter M., Siegal G., Wuthrich K. Structural role of a buried salt bridge in the 434 repressor DNA-binding domain. J. Mol. Biol. 264:1996;1002-1012.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1002-1012
    • Pervushin, K.1    Billeter, M.2    Siegal, G.3    Wuthrich, K.4
  • 29
    • 33845280446 scopus 로고
    • Comparing the polarities of the amino acids: Side-chain distribution coefficients between the vapor phase, cylclohexane, 1-octanol and neutral aqueous solution
    • Radzicka A., Wolfenden R. Comparing the polarities of the amino acids: side-chain distribution coefficients between the vapor phase, cylclohexane, 1-octanol and neutral aqueous solution. Biochemistry. 27:1988;1664-1670.
    • (1988) Biochemistry , vol.27 , pp. 1664-1670
    • Radzicka, A.1    Wolfenden, R.2
  • 30
    • 0025093185 scopus 로고
    • Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double mutant cycles
    • Serrano L., Horovitz A., Avron B., Bycroft M., Fersht A. R. Estimating the contribution of engineered surface electrostatic interactions to protein stability by using double mutant cycles. Biochemistry. 29:1990;9343-9352.
    • (1990) Biochemistry , vol.29 , pp. 9343-9352
    • Serrano, L.1    Horovitz, A.2    Avron, B.3    Bycroft, M.4    Fersht, A.R.5
  • 31
    • 0025283002 scopus 로고
    • Electrostatic interactions in macromolecules: Theory and applications
    • Sharp K. A., Honig B. Electrostatic interactions in macromolecules: theory and applications. Annu. Rev. Biophys. Biophys. Chem. 19:1990;301-332.
    • (1990) Annu. Rev. Biophys. Biophys. Chem. , vol.19 , pp. 301-332
    • Sharp, K.A.1    Honig, B.2
  • 32
    • 0024026370 scopus 로고
    • Probing the salt bridge in the dihydrofolate reductase-methotrexate complex by using the coordinate-coupled free energy perturbation method
    • Singh U. C. Probing the salt bridge in the dihydrofolate reductase-methotrexate complex by using the coordinate-coupled free energy perturbation method. Proc. Natl Acad. Sci. USA. 85:1988;4280-4284.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4280-4284
    • Singh, U.C.1
  • 33
    • 32844457567 scopus 로고
    • Accurate calculation of hydration free energies using macroscopic solvent models
    • Sitkoff D., Sharp K. A., Honig B. Accurate calculation of hydration free energies using macroscopic solvent models. J. Phys. Chem. 98:1994;1978-1988.
    • (1994) J. Phys. Chem. , vol.98 , pp. 1978-1988
    • Sitkoff, D.1    Sharp, K.A.2    Honig, B.3
  • 34
    • 0025718955 scopus 로고
    • Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis
    • Sun D. P., Sauer U., Nicholson H., Matthews B. W. Contributions of engineered surface salt bridges to the stability of T4 lysozyme determined by directed mutagenesis. Biochemistry. 30:1991;7142-7153.
    • (1991) Biochemistry , vol.30 , pp. 7142-7153
    • Sun, D.P.1    Sauer, U.2    Nicholson, H.3    Matthews, B.W.4
  • 35
    • 0031764838 scopus 로고    scopus 로고
    • Surface salt bridges stabilize the GCN4 leucine zipper
    • Spek E. J., Bui A. H., Lu M., Kallenbach N. R. Surface salt bridges stabilize the GCN4 leucine zipper. Protein Sci. 11:1998;2431-2437.
    • (1998) Protein Sci. , vol.11 , pp. 2431-2437
    • Spek, E.J.1    Bui, A.H.2    Lu, M.3    Kallenbach, N.R.4
  • 36
    • 0031012563 scopus 로고    scopus 로고
    • Hydrophobic folding units derived from dissimilar monomer structures and their interactions
    • Tsai C. J., Nussinov R. Hydrophobic folding units derived from dissimilar monomer structures and their interactions. Protein Sci. 6:1997;24-42.
    • (1997) Protein Sci. , vol.6 , pp. 24-42
    • Tsai, C.J.1    Nussinov, R.2
  • 37
    • 0030602896 scopus 로고    scopus 로고
    • A dataset of protein-protein interfaces generated with a sequence order independent comparison technique
    • Tsai C. J., Lin S. L., Wolfson H., Nussinov R. A dataset of protein-protein interfaces generated with a sequence order independent comparison technique. J. Mol. Biol. 260:1996;604-620.
    • (1996) J. Mol. Biol. , vol.260 , pp. 604-620
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.3    Nussinov, R.4
  • 38
    • 1842405464 scopus 로고    scopus 로고
    • Studies of protein-protein interfaces: A statistical analysis of the hydrophobic effect
    • Tsai C. J., Lin S. L., Wolfson H. J., Nussinov R. Studies of protein-protein interfaces: a statistical analysis of the hydrophobic effect. Protein Sci. 6:1997;53-64.
    • (1997) Protein Sci. , vol.6 , pp. 53-64
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 39
    • 0033056708 scopus 로고    scopus 로고
    • Folding funnels, binding funnels and protein function
    • Tsai C. J., Kumar S., Ma B., Nussinov R. Folding funnels, binding funnels and protein function. Protein Sci. 8:1999;1179-1188.
    • (1999) Protein Sci. , vol.8 , pp. 1179-1188
    • Tsai, C.J.1    Kumar, S.2    Ma, B.3    Nussinov, R.4
  • 40
    • 0029564595 scopus 로고
    • Are buried salt bridges important for protein stability and conformational specificity?
    • Waldburger C. D., Schildbach J. F., Sauer R. T. Are buried salt bridges important for protein stability and conformational specificity? Nature Struct. Biol. 2:1995;122-128.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 122-128
    • Waldburger, C.D.1    Schildbach, J.F.2    Sauer, R.T.3
  • 41
    • 0029966342 scopus 로고    scopus 로고
    • Barriers to protein folding: Formation of buried polar interactions is a slow step in acquisition of structure
    • Waldburger C. D., Jonsson T., Sauer R. T. Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structure. Biochemistry. 93:1996;2629-2634.
    • (1996) Biochemistry , vol.93 , pp. 2629-2634
    • Waldburger, C.D.1    Jonsson, T.2    Sauer, R.T.3
  • 42
    • 0033603392 scopus 로고    scopus 로고
    • Electrostatic contributions to the stability of hyperthermophilic proteins
    • Xiao L., Honig B. Electrostatic contributions to the stability of hyperthermophilic proteins. J. Mol. Biol. 289:1999;1435-1444.
    • (1999) J. Mol. Biol. , vol.289 , pp. 1435-1444
    • Xiao, L.1    Honig, B.2
  • 43
    • 0031450506 scopus 로고    scopus 로고
    • Hydrogen bonds and salt bridges across protein-protein interfaces
    • Xu D., Tsai C. J., Nussinov R. Hydrogen bonds and salt bridges across protein-protein interfaces. Protein Eng. 10:1997a;999-1012.
    • (1997) Protein Eng. , vol.10 , pp. 999-1012
    • Xu, D.1    Tsai, C.J.2    Nussinov, R.3
  • 44
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu D., Lin S. L., Nussinov R. Protein binding versus protein folding: the role of hydrophilic bridges in protein associations. J. Mol. Biol. 265:1997b;68-84.
    • (1997) J. Mol. Biol. , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3


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