메뉴 건너뛰기




Volumn 100, Issue 1-3, 2002, Pages 239-260

Group additivity schemes for the calculation of the partial molar heat capacities and volumes of unfolded proteins in aqueous solution

Author keywords

Additivity schemes; Heat capacity; Model compounds; Oligopeptides; Tripeptides; Unfolded proteins; Volume

Indexed keywords

AMINO ACID; CHYMOTRYPSINOGEN; CYTOCHROME C; PEPTIDE; PROTEIN; RIBONUCLEASE A;

EID: 0037438353     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00284-3     Document Type: Article
Times cited : (50)

References (67)
  • 1
    • 0012372449 scopus 로고
    • Über das molekulare Lösungvolumen und Molekularvolumen organischer Verbindungen
    • Traube J. Über das molekulare Lösungvolumen und Molekularvolumen organischer Verbindungen. Liebigs Ann. Chem. 290:1896;43-122.
    • (1896) Liebigs Ann. Chem. , vol.290 , pp. 43-122
    • Traube, J.1
  • 2
    • 33847804338 scopus 로고
    • Volumetric properties of aqueous solutions of organic compounds. III. Aliphatic secondary alcohols, cyclic alcohols, primary, secondary, and tertiary amines
    • Cabani S., Conti G., Lepori L. Volumetric properties of aqueous solutions of organic compounds. III. Aliphatic secondary alcohols, cyclic alcohols, primary, secondary, and tertiary amines. J. Phys. Chem. 78:1974;1030-1034.
    • (1974) J. Phys. Chem. , vol.78 , pp. 1030-1034
    • Cabani, S.1    Conti, G.2    Lepori, L.3
  • 3
    • 9944232242 scopus 로고
    • Group contributions to the thermodynamic properties of non-ionic organic solutes in dilute aqueous solution
    • Cabani S., Gianni P., Mollica V., Lepori L. Group contributions to the thermodynamic properties of non-ionic organic solutes in dilute aqueous solution. J. Solut. Chem. 10:1981;563-595.
    • (1981) J. Solut. Chem. , vol.10 , pp. 563-595
    • Cabani, S.1    Gianni, P.2    Mollica, V.3    Lepori, L.4
  • 4
    • 0002292014 scopus 로고
    • Partial molar volumes of biochemical model compounds in aqueous solution
    • H.-J. Hinz. Berlin: Springer-Verlag. p. 17
    • Høiland H. Partial molar volumes of biochemical model compounds in aqueous solution. Hinz H.-J. Thermodynamic Data for Biochemistry and Biotechnology. 1986;Springer-Verlag, Berlin. p. 17.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology
    • Høiland, H.1
  • 5
    • 0000542047 scopus 로고
    • Thermodynamic properties of aqueous organic solutes in relation to their structure. Part III. Apparent molal volumes and heat capacities of low molecular weight alcohols and polyols at 25 °C
    • Jolicoeur C., Lacroix G. Thermodynamic properties of aqueous organic solutes in relation to their structure. Part III. Apparent molal volumes and heat capacities of low molecular weight alcohols and polyols at 25 °C. Can. J. Chem. 54:1976;624-631.
    • (1976) Can. J. Chem. , vol.54 , pp. 624-631
    • Jolicoeur, C.1    Lacroix, G.2
  • 6
    • 0012452156 scopus 로고
    • Additivity schemes permitting the estimation of partial molar heat capacities of organic compounds in aqueous solution
    • Guthrie J.P. Additivity schemes permitting the estimation of partial molar heat capacities of organic compounds in aqueous solution. Can. J. Chem. 55:1977;3700-3706.
    • (1977) Can. J. Chem. , vol.55 , pp. 3700-3706
    • Guthrie, J.P.1
  • 7
    • 49549135017 scopus 로고
    • Additivity relations for the heat capacities of non-electrolytes in aqueous solution
    • Nichols N., Sköld R., Spink C., Suurkuusk J., Wadsö I. Additivity relations for the heat capacities of non-electrolytes in aqueous solution. J. Chem. Thermodyn. 8:1976;1081-1093.
    • (1976) J. Chem. Thermodyn. , vol.8 , pp. 1081-1093
    • Nichols, N.1    Sköld, R.2    Spink, C.3    Suurkuusk, J.4    Wadsö, I.5
  • 9
    • 0000773271 scopus 로고
    • Estimation of heats of formation of organic compounds by additivity methods
    • Cohen N., Benson S.W. Estimation of heats of formation of organic compounds by additivity methods. Chem. Rev. 93:1993;2419-2438.
    • (1993) Chem. Rev. , vol.93 , pp. 2419-2438
    • Cohen, N.1    Benson, S.W.2
  • 10
    • 0034349019 scopus 로고    scopus 로고
    • Partial molar volumes of ionic and non-ionic organic solutes in water: A simple additivity scheme based on the intrinsic volume approach
    • Lepori L., Gianni P. Partial molar volumes of ionic and non-ionic organic solutes in water: a simple additivity scheme based on the intrinsic volume approach. J. Solut. Chem. 29:2000;405-447.
    • (2000) J. Solut. Chem. , vol.29 , pp. 405-447
    • Lepori, L.1    Gianni, P.2
  • 11
    • 0030787855 scopus 로고    scopus 로고
    • Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: Additivity scheme and implication of protein unfolding at normal and high pressure
    • Kharakoz D.P. Partial volumes and compressibilities of extended polypeptide chains in aqueous solution: additivity scheme and implication of protein unfolding at normal and high pressure. Biochemistry. 36:1997;10276-10285.
    • (1997) Biochemistry , vol.36 , pp. 10276-10285
    • Kharakoz, D.P.1
  • 12
    • 0001133725 scopus 로고    scopus 로고
    • Calculation of partial specific volumes and other volumetric properties of small molecules and polymers
    • Durchschlag H., Zipper P. Calculation of partial specific volumes and other volumetric properties of small molecules and polymers. J. Appl. Cryst. 30:1997;803-807.
    • (1997) J. Appl. Cryst. , vol.30 , pp. 803-807
    • Durchschlag, H.1    Zipper, P.2
  • 13
    • 0017430379 scopus 로고
    • Heat capacities of liquid hydrocarbons. Estimation of heat capacities at constant pressure as a temperature function, using additivity rules
    • Luria M., Benson S.W. Heat capacities of liquid hydrocarbons. Estimation of heat capacities at constant pressure as a temperature function, using additivity rules. J. Chem. Eng. Data. 22:1977;90-100.
    • (1977) J. Chem. Eng. Data , vol.22 , pp. 90-100
    • Luria, M.1    Benson, S.W.2
  • 14
    • 0029874816 scopus 로고    scopus 로고
    • Group additivity analysis of the heat capacity changes associated with the dissolution into water of different organic compounds
    • Graziano G., Barone G. Group additivity analysis of the heat capacity changes associated with the dissolution into water of different organic compounds. J. Am. Chem. Soc. 118:1996;1831-1835.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 1831-1835
    • Graziano, G.1    Barone, G.2
  • 17
    • 0021195067 scopus 로고
    • Amino acid, peptide, and protein volume in solution
    • Zamyatnin A.A. Amino acid, peptide, and protein volume in solution. Annu. Rev. Biophys. Bioeng. 13:1984;145-165.
    • (1984) Annu. Rev. Biophys. Bioeng. , vol.13 , pp. 145-165
    • Zamyatnin, A.A.1
  • 18
    • 0024296532 scopus 로고
    • Implications of protein folding. Additivity schemes for volumes and compressibilities
    • Iqbal M., Verrall R.E. Implications of protein folding. Additivity schemes for volumes and compressibilities. J. Biol. Chem. 263:1988;4159-4165.
    • (1988) J. Biol. Chem. , vol.263 , pp. 4159-4165
    • Iqbal, M.1    Verrall, R.E.2
  • 19
    • 0025610122 scopus 로고
    • Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range
    • Makhatadze G.I., Medvedkin V.N., Privalov P.L. Partial molar volumes of polypeptides and their constituent groups in aqueous solution over a broad temperature range. Biopolymers. 30:1990;1001-1010.
    • (1990) Biopolymers , vol.30 , pp. 1001-1010
    • Makhatadze, G.I.1    Medvedkin, V.N.2    Privalov, P.L.3
  • 20
    • 0037605067 scopus 로고    scopus 로고
    • Partial molar volumes of proteins: Amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 °C
    • Häckel M., Hinz H.-J., Hedwig G.R. Partial molar volumes of proteins: amino acid side-chain contributions derived from the partial molar volumes of some tripeptides over the temperature range 10-90 °C. Biophys. Chem. 82:1999;35-50.
    • (1999) Biophys. Chem. , vol.82 , pp. 35-50
    • Häckel, M.1    Hinz, H.-J.2    Hedwig, G.R.3
  • 21
    • 0034646794 scopus 로고    scopus 로고
    • Calculation of the standard molal thermodynamic properties of aqueous biomolecules at elevated temperatures and pressures II. Unfolded proteins
    • Amend J.P., Helgeson H.C. Calculation of the standard molal thermodynamic properties of aqueous biomolecules at elevated temperatures and pressures II. Unfolded proteins. Biophys. Chem. 84:2000;105-136.
    • (2000) Biophys. Chem. , vol.84 , pp. 105-136
    • Amend, J.P.1    Helgeson, H.C.2
  • 22
    • 0025360593 scopus 로고
    • Heat capacity of proteins I. Partial molar heat capacity of individual amino acid residues in aqueous solution: Hydration effect
    • Makhatadze G.I., Privalov P.L. Heat capacity of proteins I. Partial molar heat capacity of individual amino acid residues in aqueous solution: hydration effect. J. Mol. Biol. 213:1990;375-384.
    • (1990) J. Mol. Biol. , vol.213 , pp. 375-384
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 23
    • 0037943192 scopus 로고    scopus 로고
    • A new set of peptide-based group heat capacities for use in protein stability calculations
    • Häckel M., Hinz H.-J., Hedwig G.R. A new set of peptide-based group heat capacities for use in protein stability calculations. J. Mol. Biol. 291:1999;197-213.
    • (1999) J. Mol. Biol. , vol.291 , pp. 197-213
    • Häckel, M.1    Hinz, H.-J.2    Hedwig, G.R.3
  • 24
    • 0018588511 scopus 로고
    • Stability of small globular proteins
    • Privalov P.L. Stability of small globular proteins. Adv. Protein Chem. 33:1979;167-237.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-237
    • Privalov, P.L.1
  • 26
    • 0030320442 scopus 로고    scopus 로고
    • The concept of a random coil. Residual structure in peptides and denatured proteins
    • Smith L.J., Fiebig K.M., Schwalbe H., Dobson C.M. The concept of a random coil. Residual structure in peptides and denatured proteins. Fold. Design. 1:1996;R95-R106.
    • (1996) Fold. Design , vol.1
    • Smith, L.J.1    Fiebig, K.M.2    Schwalbe, H.3    Dobson, C.M.4
  • 27
    • 0041022126 scopus 로고    scopus 로고
    • Tripeptides in aqueous solution: Model compounds for the evaluation of the partial molar heat capacities of the amino-acid side chains in proteins
    • Häckel M., Hinz H.-J., Hedwig G.R. Tripeptides in aqueous solution: model compounds for the evaluation of the partial molar heat capacities of the amino-acid side chains in proteins. Thermochim. Acta. 308:1998;23-34.
    • (1998) Thermochim. Acta , vol.308 , pp. 23-34
    • Häckel, M.1    Hinz, H.-J.2    Hedwig, G.R.3
  • 28
    • 0001501863 scopus 로고
    • Thermodynamic properties of peptide solutions. Part 6. The amino acid side-chain contributions to the partial molar volumes and heat capacities of some tripeptides in aqueous solution
    • Reading J.F., Hedwig G.R. Thermodynamic properties of peptide solutions. Part 6. The amino acid side-chain contributions to the partial molar volumes and heat capacities of some tripeptides in aqueous solution. J. Chem. Soc. Faraday Trans. 86:1990;3117-3123.
    • (1990) J. Chem. Soc. Faraday Trans. , vol.86 , pp. 3117-3123
    • Reading, J.F.1    Hedwig, G.R.2
  • 29
    • 0039283337 scopus 로고    scopus 로고
    • The partial molar heat capacity and volume of the peptide backbone group of proteins in aqueous solution
    • Häckel M., Hedwig G.R., Hinz H.-J. The partial molar heat capacity and volume of the peptide backbone group of proteins in aqueous solution. Biophys. Chem. 73:1998;163-177.
    • (1998) Biophys. Chem. , vol.73 , pp. 163-177
    • Häckel, M.1    Hedwig, G.R.2    Hinz, H.-J.3
  • 30
    • 0001514917 scopus 로고
    • Partial molar volumes, expansibilities, and compressibilities of α,ω-aminocarboxylic acids in aqueous solution between 18 and 55 °C
    • Chalikian T.V., Sarvazyan A.P., Breslauer K.J. Partial molar volumes, expansibilities, and compressibilities of α,ω-aminocarboxylic acids in aqueous solution between 18 and 55 °C. J. Phys. Chem. 97:1993;13017-13026.
    • (1993) J. Phys. Chem. , vol.97 , pp. 13017-13026
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 31
    • 0028413422 scopus 로고
    • Partial molar volumes expansibilities and compressibilities of oligoglycines in aqueous solution at 18-55 °C
    • Chalikian T.V., Sarvazyan A.P., Funck T., Breslauer K.J. Partial molar volumes expansibilities and compressibilities of oligoglycines in aqueous solution at 18-55 °C. Biopolymers. 34:1994;541-553.
    • (1994) Biopolymers , vol.34 , pp. 541-553
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Funck, T.3    Breslauer, K.J.4
  • 32
    • 0034541510 scopus 로고    scopus 로고
    • Additivity of the partial molar heat capacities of the amino-acid side chains of small peptides: Implications for unfolded proteins
    • Häckel M., Hinz H.-J., Hedwig G.R. Additivity of the partial molar heat capacities of the amino-acid side chains of small peptides: implications for unfolded proteins. Phys. Chem. Chem. Phys. 2:2000;5463-5468.
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 5463-5468
    • Häckel, M.1    Hinz, H.-J.2    Hedwig, G.R.3
  • 33
    • 0035528811 scopus 로고    scopus 로고
    • Apparent and partial molar heat capacities and volumes of the amino acids L-lysine monohydrochloride and L-arginine monohydrochloride in aqueous solution at temperatures from T=288.15 K to T=328.15 K
    • Hakin A.W., Hedwig G.R. Apparent and partial molar heat capacities and volumes of the amino acids L-lysine monohydrochloride and L-arginine monohydrochloride in aqueous solution at temperatures from T=288.15 K to T=328.15 K. J. Chem. Thermodyn. 33:2001;1709-1723.
    • (2001) J. Chem. Thermodyn. , vol.33 , pp. 1709-1723
    • Hakin, A.W.1    Hedwig, G.R.2
  • 35
    • 0034655349 scopus 로고    scopus 로고
    • The partial molar heat capacities and volumes of some N-acetyl amino acid amides in aqueous solution over the temperature range 288.15 to 328.15 K
    • Hakin A.W., Hedwig G.R. The partial molar heat capacities and volumes of some N-acetyl amino acid amides in aqueous solution over the temperature range 288.15 to 328.15 K. Phys. Chem. Chem. Phys. 2:2000;1795-1802.
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 1795-1802
    • Hakin, A.W.1    Hedwig, G.R.2
  • 36
    • 0035471081 scopus 로고    scopus 로고
    • Amino acid derivatives as protein side-chain model compounds: The partial molar volumes and heat capacities of some N-acetyl-N′-methyl amino acid amides in aqueous solution
    • Liu J.L., Hakin A.W., Hedwig G.R. Amino acid derivatives as protein side-chain model compounds: the partial molar volumes and heat capacities of some N-acetyl-N′-methyl amino acid amides in aqueous solution. J. Solut. Chem. 30:2001;861-883.
    • (2001) J. Solut. Chem. , vol.30 , pp. 861-883
    • Liu, J.L.1    Hakin, A.W.2    Hedwig, G.R.3
  • 37
    • 0000725989 scopus 로고
    • Some thermodynamic properties of aqueous amino acid systems at 288.15, 298.15, 313.15 and 328.15 K: Group additivity analysis of standard-state volumes and heat capacities
    • Hakin A.W., Duke M.M., Marty J.L., Preuss K.E. Some thermodynamic properties of aqueous amino acid systems at 288.15, 298.15, 313.15 and 328.15 K: group additivity analysis of standard-state volumes and heat capacities. J. Chem. Soc. Faraday Trans. 90:1994;2027-2035.
    • (1994) J. Chem. Soc. Faraday Trans. , vol.90 , pp. 2027-2035
    • Hakin, A.W.1    Duke, M.M.2    Marty, J.L.3    Preuss, K.E.4
  • 38
    • 0028369444 scopus 로고
    • Apparent molar heat capacities and volumes of some aliphatic amino acids at 288.15, 298.15, 313.15, and 328.15 K
    • Hakin A.W., Duke M.M., Klassen S.A., McKay R.M., Preuss K.E. Apparent molar heat capacities and volumes of some aliphatic amino acids at 288.15, 298.15, 313.15, and 328.15 K. Can. J. Chem. 72:1994;362-368.
    • (1994) Can. J. Chem. , vol.72 , pp. 362-368
    • Hakin, A.W.1    Duke, M.M.2    Klassen, S.A.3    McKay, R.M.4    Preuss, K.E.5
  • 39
    • 0035865621 scopus 로고    scopus 로고
    • Group additivity calculations of the thermodynamic properties of unfolded proteins in aqueous solution: A critical comparison of peptide-based and HKF models
    • Hakin A.W., Hedwig G.R. Group additivity calculations of the thermodynamic properties of unfolded proteins in aqueous solution: a critical comparison of peptide-based and HKF models. Biophys. Chem. 89:2001;253-264.
    • (2001) Biophys. Chem. , vol.89 , pp. 253-264
    • Hakin, A.W.1    Hedwig, G.R.2
  • 40
    • 0034327382 scopus 로고    scopus 로고
    • The partial molar volumes of some tetra- and pentapeptides in aqueous solution: A test of amino acid side-chain group additivity for unfolded proteins
    • Häckel M., Hinz H.-J., Hedwig G.R. The partial molar volumes of some tetra- and pentapeptides in aqueous solution: a test of amino acid side-chain group additivity for unfolded proteins. Phys. Chem. Chem. Phys. 2:2000;4843-4849.
    • (2000) Phys. Chem. Chem. Phys. , vol.2 , pp. 4843-4849
    • Häckel, M.1    Hinz, H.-J.2    Hedwig, G.R.3
  • 41
    • 0027967921 scopus 로고
    • An alternative interpretation of the heat capacity changes associated with protein unfolding
    • Hinz H.-J., Vogl T., Meyer R. An alternative interpretation of the heat capacity changes associated with protein unfolding. Biophys. Chem. 52:1994;275-285.
    • (1994) Biophys. Chem. , vol.52 , pp. 275-285
    • Hinz, H.-J.1    Vogl, T.2    Meyer, R.3
  • 42
    • 37049087272 scopus 로고
    • Partial molar heat capacities and volumes of aqueous solutions of some peptides that model side-chains of proteins
    • Hedwig G.R. Partial molar heat capacities and volumes of aqueous solutions of some peptides that model side-chains of proteins. J. Chem. Soc. Faraday Trans. 89:1993;2761-2768.
    • (1993) J. Chem. Soc. Faraday Trans. , vol.89 , pp. 2761-2768
    • Hedwig, G.R.1
  • 43
    • 0032070440 scopus 로고    scopus 로고
    • Thermodynamic properties of peptide solutions. Part 16. Partial molar heat capacities and volumes of some tripeptides of sequence Gly-X-Gly in aqueous solution at 25 °C
    • Schwitzer M.A., Hedwig G.R. Thermodynamic properties of peptide solutions. Part 16. Partial molar heat capacities and volumes of some tripeptides of sequence Gly-X-Gly in aqueous solution at 25 °C. J. Chem. Eng. Data. 43:1998;477-481.
    • (1998) J. Chem. Eng. Data , vol.43 , pp. 477-481
    • Schwitzer, M.A.1    Hedwig, G.R.2
  • 44
    • 37049081294 scopus 로고
    • Thermodynamics of solvation of ions. 6. The standard partial molar volumes of aqueous ions at 298.15 K
    • Marcus Y. Thermodynamics of solvation of ions. 6. The standard partial molar volumes of aqueous ions at 298.15 K. J. Chem. Soc. Faraday Trans. 89:1993;713-718.
    • (1993) J. Chem. Soc. Faraday Trans. , vol.89 , pp. 713-718
    • Marcus, Y.1
  • 45
    • 4143090195 scopus 로고
    • The evaluation and use of properties of individual ions in solution
    • Conway B.E. The evaluation and use of properties of individual ions in solution. J. Solut. Chem. 7:1978;721-770.
    • (1978) J. Solut. Chem. , vol.7 , pp. 721-770
    • Conway, B.E.1
  • 47
    • 0030367392 scopus 로고    scopus 로고
    • Apparent molar volumes of 1-pentanol in water from T=298 K to T=413 K at p=0.1 MPa and p=19 MPa
    • Inglese A., Robert P., De Lisi R., Milioto S. Apparent molar volumes of 1-pentanol in water from T=298 K to T=413 K at p=0.1 MPa and p=19 MPa. J. Chem. Thermodyn. 28:1996;873-886.
    • (1996) J. Chem. Thermodyn. , vol.28 , pp. 873-886
    • Inglese, A.1    Robert, P.2    De Lisi, R.3    Milioto, S.4
  • 48
    • 0000623052 scopus 로고
    • Volumetric properties of dilute aqueous alcohol solutions at different temperatures
    • Sakurai M., Nakamura K., Nitta K. Volumetric properties of dilute aqueous alcohol solutions at different temperatures. Bull. Chem. Soc. Jpn. 67:1994;1580-1587.
    • (1994) Bull. Chem. Soc. Jpn. , vol.67 , pp. 1580-1587
    • Sakurai, M.1    Nakamura, K.2    Nitta, K.3
  • 49
    • 0001621306 scopus 로고
    • PVT properties of concentrated aqueous electrolytes: V. Densities and apparent molal volumes of the four major sea salts from dilute solutions to saturation and from 0 to 100 °C
    • Connaughton L.M., Hershey J.P., Millero F.J. PVT properties of concentrated aqueous electrolytes: V. Densities and apparent molal volumes of the four major sea salts from dilute solutions to saturation and from 0 to 100 °C. J. Solut. Chem. 15:1986;989-1002.
    • (1986) J. Solut. Chem. , vol.15 , pp. 989-1002
    • Connaughton, L.M.1    Hershey, J.P.2    Millero, F.J.3
  • 50
    • 0030376854 scopus 로고    scopus 로고
    • Volumes and heat capacities of aqueous solutions of ammonium chloride from the temperatures 298.15 K to 623 K and pressures to 28 MPa
    • Sharygin A.V., Wood R.H. Volumes and heat capacities of aqueous solutions of ammonium chloride from the temperatures 298.15 K to 623 K and pressures to 28 MPa. J. Chem. Thermodyn. 28:1996;851-872.
    • (1996) J. Chem. Thermodyn. , vol.28 , pp. 851-872
    • Sharygin, A.V.1    Wood, R.H.2
  • 51
    • 0030376983 scopus 로고    scopus 로고
    • Apparent molar volumes of aqueous solutions of some organic solutes at the pressure 28 MPa and temperatures to 598 K
    • Criss C.M., Wood R.H. Apparent molar volumes of aqueous solutions of some organic solutes at the pressure 28 MPa and temperatures to 598 K. J. Chem. Thermodyn. 28:1996;723-741.
    • (1996) J. Chem. Thermodyn. , vol.28 , pp. 723-741
    • Criss, C.M.1    Wood, R.H.2
  • 52
    • 46149133894 scopus 로고
    • Apparent molar volumes, isobaric expansion coefficients, and isentropic compressibilities, and their H/D isotope effects for some aqueous carbohydrate solutions
    • Bernal P.J., Van Hook W.A. Apparent molar volumes, isobaric expansion coefficients, and isentropic compressibilities, and their H/D isotope effects for some aqueous carbohydrate solutions. J. Chem. Thermodyn. 18:1986;955-968.
    • (1986) J. Chem. Thermodyn. , vol.18 , pp. 955-968
    • Bernal, P.J.1    Van Hook, W.A.2
  • 54
    • 84990436498 scopus 로고
    • Aqueous solutions containing amino acids and peptides. Part 20. Volumetric behaviour of some terminally substituted amino acids and peptides at 298.15 K
    • Leslie T.E., Lilley T.H. Aqueous solutions containing amino acids and peptides. Part 20. Volumetric behaviour of some terminally substituted amino acids and peptides at 298.15 K. Biopolymers. 24:1985;695-710.
    • (1985) Biopolymers , vol.24 , pp. 695-710
    • Leslie, T.E.1    Lilley, T.H.2
  • 55
    • 0030837446 scopus 로고    scopus 로고
    • Group additivity equations of state for calculating the standard molal thermodynamic properties of aqueous organic species at elevated temperatures and pressures
    • Amend J.P., Helgeson H.C. Group additivity equations of state for calculating the standard molal thermodynamic properties of aqueous organic species at elevated temperatures and pressures. Geochim. Cosmochim. Acta. 61:1997;11-46.
    • (1997) Geochim. Cosmochim. Acta , vol.61 , pp. 11-46
    • Amend, J.P.1    Helgeson, H.C.2
  • 56
    • 33748638848 scopus 로고    scopus 로고
    • Calculation of the standard molal thermodynamic properties of aqueous biomolecules at elevated temperatures and pressures. Part 1. L-α-Amino acids
    • Amend J.P., Helgeson H.C. Calculation of the standard molal thermodynamic properties of aqueous biomolecules at elevated temperatures and pressures. Part 1. L-α-Amino acids. J. Chem. Soc. Faraday Trans. 93:1997;1927-1941.
    • (1997) J. Chem. Soc. Faraday Trans. , vol.93 , pp. 1927-1941
    • Amend, J.P.1    Helgeson, H.C.2
  • 57
    • 0025207061 scopus 로고
    • Calculation of the thermodynamic and transport properties of aqueous species at high pressures and temperatures: Standard partial molal properties of organic species
    • Shock E.L., Helgeson H.C. Calculation of the thermodynamic and transport properties of aqueous species at high pressures and temperatures: standard partial molal properties of organic species. Geochim. Cosmochim. Acta. 54:1990;915-945.
    • (1990) Geochim. Cosmochim. Acta , vol.54 , pp. 915-945
    • Shock, E.L.1    Helgeson, H.C.2
  • 59
    • 33845377574 scopus 로고
    • Partial molar heat capacities and volumes of transfer of some amino acids and peptides from water to aqueous sodium chloride solutions at 298.15 K
    • Bhat R., Ahluwalia J.C. Partial molar heat capacities and volumes of transfer of some amino acids and peptides from water to aqueous sodium chloride solutions at 298.15 K. J. Phys. Chem. 89:1985;1099-1105.
    • (1985) J. Phys. Chem. , vol.89 , pp. 1099-1105
    • Bhat, R.1    Ahluwalia, J.C.2
  • 60
    • 0030699525 scopus 로고    scopus 로고
    • A circular dichrosim study of preferential hydration and alcohol effects on denatured protein, pig calpastatin domain I
    • Konno T., Tanaka N., Kataoka M., Takano E., Maki M. A circular dichrosim study of preferential hydration and alcohol effects on denatured protein, pig calpastatin domain I. Biochim. Biophys. Acta. 1342:1997;73-82.
    • (1997) Biochim. Biophys. Acta , vol.1342 , pp. 73-82
    • Konno, T.1    Tanaka, N.2    Kataoka, M.3    Takano, E.4    Maki, M.5
  • 61
    • 0342264518 scopus 로고    scopus 로고
    • A new alternative method to quantify residual structure in 'unfolded' proteins
    • Häckel M., Konno T., Hinz H.-J. A new alternative method to quantify residual structure in 'unfolded' proteins. Biochim. Biophys. Acta. 1479:2000;155-165.
    • (2000) Biochim. Biophys. Acta , vol.1479 , pp. 155-165
    • Häckel, M.1    Konno, T.2    Hinz, H.-J.3
  • 62
    • 33845561444 scopus 로고
    • Compressibility of globular proteins in water at 25 °C
    • Gekko K., Noguchi H. Compressibility of globular proteins in water at 25 °C. J. Phys. Chem. 83:1979;2706-2714.
    • (1979) J. Phys. Chem. , vol.83 , pp. 2706-2714
    • Gekko, K.1    Noguchi, H.2
  • 63
    • 0008047756 scopus 로고    scopus 로고
    • The hydration of globular proteins as derived from volume and compressibility measurements: Cross-correlating thermodynamic and structural data
    • Chalikian T.V., Totrov M., Abagyan R., Breslauer K.J. The hydration of globular proteins as derived from volume and compressibility measurements: cross-correlating thermodynamic and structural data. J. Mol. Biol. 260:1996;588-603.
    • (1996) J. Mol. Biol. , vol.260 , pp. 588-603
    • Chalikian, T.V.1    Totrov, M.2    Abagyan, R.3    Breslauer, K.J.4
  • 64
    • 0022999267 scopus 로고
    • Compressibility-structure relationship of globular proteins
    • Gekko K., Hasegawa Y. Compressibility-structure relationship of globular proteins. Biochemistry. 25:1986;6563-6571.
    • (1986) Biochemistry , vol.25 , pp. 6563-6571
    • Gekko, K.1    Hasegawa, Y.2
  • 65
    • 0030298077 scopus 로고    scopus 로고
    • On volume changes accompanying conformational transitions of biopolymers
    • Chalikian T.V., Breslauer K.J. On volume changes accompanying conformational transitions of biopolymers. Biopolymers. 39:1996;619-625.
    • (1996) Biopolymers , vol.39 , pp. 619-625
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 66
    • 0000092070 scopus 로고
    • Effect of temperature on the compressibility of native globular proteins
    • Gekko K., Hasegawa Y. Effect of temperature on the compressibility of native globular proteins. J. Phys. Chem. 93:1989;426-429.
    • (1989) J. Phys. Chem. , vol.93 , pp. 426-429
    • Gekko, K.1    Hasegawa, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.