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Volumn 43, Issue 5, 2004, Pages 1329-1342

Additive Transfer Free Energies of the Peptide Backbone Unit That Are Independent of the Model Compound and the Choice of Concentration Scale

Author keywords

[No Author keywords available]

Indexed keywords

ENERGY TRANSFER; FREE ENERGY; ORGANIC SOLVENTS; POLYPEPTIDES; PROTEINS;

EID: 0842304735     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035908r     Document Type: Article
Times cited : (198)

References (48)
  • 1
    • 34247513828 scopus 로고
    • Zur Lehr von der Wirkung der Salze
    • Hofmeister, F. (1888) Zur Lehr von der Wirkung der Salze, Arch. Exp. Pathol. Pharm. 24, 247-260.
    • (1888) Arch. Exp. Pathol. Pharm. , vol.24 , pp. 247-260
    • Hofmeister, F.1
  • 2
    • 0842345344 scopus 로고
    • Studies on Solubility 1: The solubility of salts in salt solutions
    • Brønsted, J. N. (1920) Studies on Solubility 1: The solubility of salts in salt solutions, J. Am. Chem. Soc. 42, 761-786.
    • (1920) J. Am. Chem. Soc. , vol.42 , pp. 761-786
    • Brønsted, J.N.1
  • 3
    • 0842302295 scopus 로고
    • The effect of salts on the solubility of other salts. I
    • Noyes, A. A., and Bray, W. C. (1911) The effect of salts on the solubility of other salts. I., J. Am. Chem. Soc. 33, 1643-1649.
    • (1911) J. Am. Chem. Soc. , vol.33 , pp. 1643-1649
    • Noyes, A.A.1    Bray, W.C.2
  • 4
    • 0842280519 scopus 로고
    • The effect of salts on the solubility of other salts. II
    • Noyes, A. A., and Bray, W. C. (1911) The effect of salts on the solubility of other salts. II., J. Am. Chem. Soc. 33, 1650-1663.
    • (1911) J. Am. Chem. Soc. , vol.33 , pp. 1650-1663
    • Noyes, A.A.1    Bray, W.C.2
  • 5
    • 0842302296 scopus 로고
    • The Activity of Electrolytes from Freezing Point Data, and Tables of Activity Coefficients, The Activity Coefficient in Mixed Electrolytes, from Solubility Measurements
    • Chapter XXVII, McGraw-Hill Book Company, Inc., New York and London
    • Lewis, G. N., and Randall, M. (1923) The Activity of Electrolytes from Freezing Point Data, and Tables of Activity Coefficients, The Activity Coefficient in Mixed Electrolytes, from Solubility Measurements in Thermodynamics and the Free Energy of Chemical Substances, Chapter XXVII, p 369, McGraw-Hill Book Company, Inc., New York and London.
    • (1923) Thermodynamics and the Free Energy of Chemical Substances , pp. 369
    • Lewis, G.N.1    Randall, M.2
  • 8
    • 0008863560 scopus 로고
    • Some Factors in the Interpretation of Protein Denaturation
    • Kauzmann, W. (1959) Some Factors in the Interpretation of Protein Denaturation, Adv. Prot. Chem. 14, 1-63.
    • (1959) Adv. Prot. Chem. , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 9
    • 78651119214 scopus 로고
    • The Solubility of Amino Acids and Related Compounds in Aqueous Urea Solutions
    • Nozaki, Y., and Tanford, C. (1963) The Solubility of Amino Acids and Related Compounds in Aqueous Urea Solutions, J. Biol. Chem. 238, 4074-4081.
    • (1963) J. Biol. Chem. , vol.238 , pp. 4074-4081
    • Nozaki, Y.1    Tanford, C.2
  • 10
    • 0014939368 scopus 로고
    • The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions
    • Nozaki, Y., and Tanford, C. (1970) The solubility of amino acids, diglycine, and triglycine in aqueous guanidine hydrochloride solutions, J. Biol. Chem. 245, 1648-1652.
    • (1970) J. Biol. Chem. , vol.245 , pp. 1648-1652
    • Nozaki, Y.1    Tanford, C.2
  • 11
    • 0001664170 scopus 로고
    • The Effect of Compounds of the Urea-Guanidinium Class on the Activity Coefficient of Acetyltetraglycine Ethyl Ester and Related Compounds
    • Robinson, D. R., and Jencks, W. P. (1965) The Effect of Compounds of the Urea-Guanidinium Class on the Activity Coefficient of Acetyltetraglycine Ethyl Ester and Related Compounds, J. Am. Chem. Soc. 87, 2462-2470.
    • (1965) J. Am. Chem. Soc. , vol.87 , pp. 2462-2470
    • Robinson, D.R.1    Jencks, W.P.2
  • 12
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • Wimley, W. C., Creamer, T. P., and White, S. H. (1996) Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides, Biochemistry 35, 5109-24.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 13
    • 0024286073 scopus 로고
    • Influences of solvent water on protein folding: Free energies of solvation of cis and trans peptides are nearly identical
    • Radzicka, A., Pedersen, L., and Wolfenden, R. (1988) Influences of solvent water on protein folding: free energies of solvation of cis and trans peptides are nearly identical, Biochemistry 27, 4538-4541.
    • (1988) Biochemistry , vol.27 , pp. 4538-4541
    • Radzicka, A.1    Pedersen, L.2    Wolfenden, R.3
  • 14
    • 0000484499 scopus 로고
    • Hydrophobic Parameters-Pi of Amino-Acid Side-Chains from the Partitioning of N-Acetyl-Amino-Acid Amides
    • Fauchere, J. L., and Pliska, V. (1983) Hydrophobic Parameters-Pi of Amino-Acid Side-Chains from the Partitioning of N-Acetyl-Amino-Acid Amides, Eur. J. Med. Chem. 18, 369-375.
    • (1983) Eur. J. Med. Chem. , vol.18 , pp. 369-375
    • Fauchere, J.L.1    Pliska, V.2
  • 16
    • 0002050426 scopus 로고
    • Conformational Transitions of Proteins in Water and in Aqueous Mixtures
    • (Timasheff, S. N., and Fasman, G. D., Eds.) Chapter 3, Marcel Dekker, Inc., New York
    • Brandts, J. F. (1969) Conformational Transitions of Proteins in Water and in Aqueous Mixtures in Structure and Stability of Biological Macromolecules (Timasheff, S. N., and Fasman, G. D., Eds.) Chapter 3, pp 213-290, Marcel Dekker, Inc., New York.
    • (1969) Structure and Stability of Biological Macromolecules , pp. 213-290
    • Brandts, J.F.1
  • 17
    • 0035237232 scopus 로고    scopus 로고
    • Protein stabilization by naturally occurring osmolytes
    • Bolen, D. W. (2001) Protein stabilization by naturally occurring osmolytes, Methods Mol. Biol. 168, 17-36.
    • (2001) Methods Mol. Biol. , vol.168 , pp. 17-36
    • Bolen, D.W.1
  • 18
    • 0028862864 scopus 로고
    • The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes
    • Liu, Y., and Bolen, D. W. (1995) The peptide backbone plays a dominant role in protein stabilization by naturally occurring osmolytes, Biochemistry 34, 12884-12891.
    • (1995) Biochemistry , vol.34 , pp. 12884-12891
    • Liu, Y.1    Bolen, D.W.2
  • 19
    • 0032483027 scopus 로고    scopus 로고
    • Osmolyte-driven contraction of a random coil protein
    • Qu, Y., Bolen, C. L., and Bolen, D. W. (1998) Osmolyte-driven contraction of a random coil protein, Proc. Natl. Acad. Sci. U.S.A. 95, 9268-9273.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 9268-9273
    • Qu, Y.1    Bolen, C.L.2    Bolen, D.W.3
  • 20
    • 0030762556 scopus 로고    scopus 로고
    • A naturally occurring protective system in urea-rich cells: Mechanism of osmolyte protection of proteins against urea denaturation
    • Wang, A., and Bolen, D. W. (1997) A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation, Biochemistry 36, 9101-9108.
    • (1997) Biochemistry , vol.36 , pp. 9101-9108
    • Wang, A.1    Bolen, D.W.2
  • 21
    • 0035958656 scopus 로고    scopus 로고
    • The osmophobic effect: Natural selection of a thermodynamic force in protein folding
    • Bolen, D. W., and Baskakov, I. V. (2001) The osmophobic effect: natural selection of a thermodynamic force in protein folding, J. Mol. Biol. 310, 955-963.
    • (2001) J. Mol. Biol. , vol.310 , pp. 955-963
    • Bolen, D.W.1    Baskakov, I.V.2
  • 22
    • 76549182497 scopus 로고
    • The solubility of amino acids and related compounds in aqueous ethylene glycol solutions
    • Nozaki, Y., and Tanford, C. (1965) The solubility of amino acids and related compounds in aqueous ethylene glycol solutions, J. Biol. Chem. 240, 3568-3575.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3568-3575
    • Nozaki, Y.1    Tanford, C.2
  • 23
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale
    • Nozaki, Y., and Tanford, C. (1971) The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale, J. Biol. Chem. 246, 2211-2217.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 24
    • 0014718113 scopus 로고
    • Protein denaturation. C. Theoretical models for the mechanism of denaturation
    • Tanford, C. (1970) Protein denaturation. C. Theoretical models for the mechanism of denaturation, Adv. Protein. Chem. 24, 1-95.
    • (1970) Adv. Protein. Chem. , vol.24 , pp. 1-95
    • Tanford, C.1
  • 25
    • 0016505899 scopus 로고
    • The Stability of Globular Proteins
    • Pace, C. N. (1975) The Stability of Globular Proteins, CRC Crit. Rev. Biochem. 3, 1-43.
    • (1975) CRC Crit. Rev. Biochem. , vol.3 , pp. 1-43
    • Pace, C.N.1
  • 26
    • 0039819615 scopus 로고
    • Thermodynamic studies of the interactions of guanidinium chloride and urea with some oligoglycines and oligoleucines
    • Lapanje, S., Skerjanc, J., Glavnik, S., and Zibret, S. (1978) Thermodynamic studies of the interactions of guanidinium chloride and urea with some oligoglycines and oligoleucines, J. Chem. Thermodyn. 10, 425-433.
    • (1978) J. Chem. Thermodyn. , vol.10 , pp. 425-433
    • Lapanje, S.1    Skerjanc, J.2    Glavnik, S.3    Zibret, S.4
  • 27
    • 0017122087 scopus 로고
    • Transfer Free Energies and Average Static Accessibilities for Ribonuclease A in Guanidinium Hydrochloride and Urea Solutions
    • Schrier, M. Y., and Schrier, E. E. (1976) Transfer Free Energies and Average Static Accessibilities for Ribonuclease A in Guanidinium Hydrochloride and Urea Solutions, Biochemistry 15, 2607-2612.
    • (1976) Biochemistry , vol.15 , pp. 2607-2612
    • Schrier, M.Y.1    Schrier, E.E.2
  • 28
    • 33947488954 scopus 로고
    • Isothermal Unfolding of Globular Proteins in Aqueous Urea Solutions
    • Tanford, C. (1964) Isothermal Unfolding of Globular Proteins in Aqueous Urea Solutions, J. Am. Chem. Soc. 86, 2050-2059.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 2050-2059
    • Tanford, C.1
  • 29
    • 33947485233 scopus 로고
    • Nonpolar Group Participation in the Denaturation of Proteins by Urea and Guanidinium Salts. Model Compound Studies
    • Wetlaufer, D. B., Malik, S. K., Stoller, L., and Coffin, R. L. (1964) Nonpolar Group Participation in the Denaturation of Proteins by Urea and Guanidinium Salts. Model Compound Studies, J. Am. Chem. Soc. 86, 508-514.
    • (1964) J. Am. Chem. Soc. , vol.86 , pp. 508-514
    • Wetlaufer, D.B.1    Malik, S.K.2    Stoller, L.3    Coffin, R.L.4
  • 30
    • 0021766648 scopus 로고
    • Effects of Urea and Guanidine-Hydrochloride on Peptide and Nonpolar Groups
    • Nandi, P. K., and Robinson, D. R. (1984) Effects of Urea and Guanidine-Hydrochloride on Peptide and Nonpolar Groups, Biochemistry 23, 6661-6668.
    • (1984) Biochemistry , vol.23 , pp. 6661-6668
    • Nandi, P.K.1    Robinson, D.R.2
  • 31
    • 3943103200 scopus 로고
    • Standard Thermodynamics of Transfer. Uses and Misuses
    • Ben-Naim, A. (1978) Standard Thermodynamics of Transfer. Uses and Misuses, J. Phys. Chem. 82, 792-803.
    • (1978) J. Phys. Chem. , vol.82 , pp. 792-803
    • Ben-Naim, A.1
  • 32
    • 84967627944 scopus 로고
    • (Coetzee, J. F., and Ritchey, C. D., Eds.) Chapter 6, Marcel Dekker, New York
    • Arnett, E., and McKelvey, D. R. (1969) in Solute-Solvent Interactions (Coetzee, J. F., and Ritchey, C. D., Eds.) Chapter 6, Marcel Dekker, New York.
    • (1969) Solute-Solvent Interactions
    • Arnett, E.1    McKelvey, D.R.2
  • 34
    • 0041743073 scopus 로고    scopus 로고
    • Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization
    • Russo, A. T., Rösgen, J., and Bolen, D. W. (2003) Osmolyte effects on kinetics of FKBP12 C22A folding coupled with prolyl isomerization, J. Mol. Biol. 330, 851-866.
    • (2003) J. Mol. Biol. , vol.330 , pp. 851-866
    • Russo, A.T.1    Rösgen, J.2    Bolen, D.W.3
  • 35
    • 0006678659 scopus 로고
    • Solubility of Diketopiperazine in Aqueous Solutions of Urea
    • Gill, S. J., Hutson, J., Clopton, J. R., and Downing, M. (1961) Solubility of Diketopiperazine in Aqueous Solutions of Urea, J. Phys. Chem. 65, 1432-1435.
    • (1961) J. Phys. Chem. , vol.65 , pp. 1432-1435
    • Gill, S.J.1    Hutson, J.2    Clopton, J.R.3    Downing, M.4
  • 36
    • 84985648217 scopus 로고
    • Thermodynamic Interaction between Urea and the Peptide Group in Aqueous Solutions at 25 °C
    • Schönert, H., and Stroth, L. (1981) Thermodynamic Interaction Between Urea and the Peptide Group in Aqueous Solutions at 25 °C, Biopolymers 20, 817-831.
    • (1981) Biopolymers , vol.20 , pp. 817-831
    • Schönert, H.1    Stroth, L.2
  • 37
    • 0006714043 scopus 로고
    • Thermodynamic Properties of Solutions of Amino Acids and Related Substances VI. The Activities of some Peptides in Aqueous Solution at Twenty-Five Degrees
    • Smith, E. R. B., and Smith, P. K. (1940) Thermodynamic Properties of Solutions of Amino Acids and Related Substances VI. The Activities of some Peptides in Aqueous Solution at Twenty-Five Degrees, J. Biol. Chem. 135, 273-279.
    • (1940) J. Biol. Chem. , vol.135 , pp. 273-279
    • Smith, E.R.B.1    Smith, P.K.2
  • 38
    • 33947481215 scopus 로고
    • Activity, Density and Relative Viscosity Data for Several Amino Acids, Lactamide, and Raffinose in Aqueous Solution at 25°
    • Ellerton, D. H., Reinfelds, G., Mulcahy, D. E., and Dunlop, P. J. (1964) Activity, Density and Relative Viscosity Data for Several Amino Acids, Lactamide, and Raffinose in Aqueous Solution at 25°, J. Phys. Chem. 68, 398-402.
    • (1964) J. Phys. Chem. , vol.68 , pp. 398-402
    • Ellerton, D.H.1    Reinfelds, G.2    Mulcahy, D.E.3    Dunlop, P.J.4
  • 39
    • 0041909097 scopus 로고
    • Activity Coefficients for the System Glycyl-glycine-Urea-Water
    • Uedaira, H. (1972) Activity Coefficients for the System Glycyl-glycine-Urea-Water, Bull. Chem. Soc. Jpn. 45, 3068-3072.
    • (1972) Bull. Chem. Soc. Jpn. , vol.45 , pp. 3068-3072
    • Uedaira, H.1
  • 40
    • 0015666339 scopus 로고
    • Thermodynamics of Hydrophobic Interaction in Systems Water+Glycine+Urea and Water+Alanine+Urea at 25 °C
    • Rafflenbeul, L., Pang, W.-M., Schönert, H., and Haberle, K. (1973) Thermodynamics of Hydrophobic Interaction in Systems Water+Glycine+Urea and Water+Alanine+Urea at 25 °C, Z. Naturforsch. 28, 533-554.
    • (1973) Z. Naturforsch. , vol.28 , pp. 533-554
    • Rafflenbeul, L.1    Pang, W.-M.2    Schönert, H.3    Haberle, K.4
  • 41
    • 0003165874 scopus 로고
    • Interactions between Amino Acids, Peptides and Related Substances, Activity Coefficients as a Function of Concentration
    • Chapter 10, Reinhold Publishing Corporation, New York
    • Cohn, E. J., and Edsall, J. T. (1943) Interactions between Amino Acids, Peptides and Related Substances, Activity Coefficients as a Function of Concentration in Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions, Chapter 10, p 231, Reinhold Publishing Corporation, New York.
    • (1943) Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions , pp. 231
    • Cohn, E.J.1    Edsall, J.T.2
  • 42
    • 0000352001 scopus 로고
    • Dielectric constants: Ethanol-Diethyl Ether and Urea-Water Solutions between 0 and 50°
    • Wyman, J. (1933) Dielectric constants: Ethanol-Diethyl Ether and Urea-Water Solutions between 0 and 50°, J. Am. Chem. Soc. 55, 4116-4121.
    • (1933) J. Am. Chem. Soc. , vol.55 , pp. 4116-4121
    • Wyman, J.1
  • 43
    • 0003165874 scopus 로고
    • Interactions between Amino Acids, Peptides and Related Substances, Activity Coefficients as a Function of Concentration
    • Chapter 10, Reinhold Publishing Corporation, New York
    • Cohn, E. J., and Edsall, J. T. (1943) Interactions between Amino Acids, Peptides and Related Substances, Activity Coefficients as a Function of Concentration in Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions, Chapter 10, p 232, Reinhold Publishing Corporation, New York.
    • (1943) Proteins, Amino Acids, and Peptides as Ions and Dipolar Ions , pp. 232
    • Cohn, E.J.1    Edsall, J.T.2
  • 47
    • 0842345346 scopus 로고
    • Effect of Denaturing Agents of the Urea-Guanidinium Class on the Solubility of Acetyltetraglycine Ethyl Ester and Related Compounds
    • Robinson, D. R., and Jencks, W. P. (1963) Effect of Denaturing Agents of the Urea-Guanidinium Class on the Solubility of Acetyltetraglycine Ethyl Ester and Related Compounds, J. Biol. Chem. 238, 1558-1560.
    • (1963) J. Biol. Chem. , vol.238 , pp. 1558-1560
    • Robinson, D.R.1    Jencks, W.P.2
  • 48
    • 0037138672 scopus 로고    scopus 로고
    • The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea
    • Zou, Q., Bennion, B. J., Daggett, V., and Murphy, K. P. (2002) The molecular mechanism of stabilization of proteins by TMAO and its ability to counteract the effects of urea, J. Am. Chem. Soc. 124, 1192-1202.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1192-1202
    • Zou, Q.1    Bennion, B.J.2    Daggett, V.3    Murphy, K.P.4


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