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Volumn 43, Issue 46, 2004, Pages 14744-14758

Preferential interactions of glycine betaine and of urea with DNA: Implications for DNA hydration and for effects of these solutes on DNA stability

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CONCENTRATION (PROCESS); DNA; NUCLEIC ACIDS; VAPOR PRESSURE;

EID: 8744318698     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049096q     Document Type: Article
Times cited : (109)

References (68)
  • 1
    • 0037465426 scopus 로고    scopus 로고
    • Thermal and urea-induced unfolding of the marginally stable lac repressor DNA-binding domain: A model system for analysis of solute effects on protein processes
    • Felitsky, D. J., and Record, M. T., Jr. (2003) Thermal and urea-induced unfolding of the marginally stable lac repressor DNA-binding domain: a model system for analysis of solute effects on protein processes, Biochemistry 42, 2202-2217.
    • (2003) Biochemistry , vol.42 , pp. 2202-2217
    • Felitsky, D.J.1    Record Jr., M.T.2
  • 2
    • 0034681955 scopus 로고    scopus 로고
    • Vapor pressure osmometry studies of osmolyte-protein interactions: Implications for the action of osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro
    • Courtenay, E. S., Capp, M. W., Anderson, C. F., and Record, M. T., Jr. (2000) Vapor pressure osmometry studies of osmolyte-protein interactions: implications for the action of osmoprotectants in vivo and for the interpretation of "osmotic stress" experiments in vitro, Biochemistry 39, 4455-4471.
    • (2000) Biochemistry , vol.39 , pp. 4455-4471
    • Courtenay, E.S.1    Capp, M.W.2    Anderson, C.F.3    Record Jr., M.T.4
  • 3
    • 0033772098 scopus 로고    scopus 로고
    • Thermodynamic analysis of interactions between denaturants and protein surface exposed on unfolding: Interpretation of urea and guanidinium chloride m-values and their correlation with changes in accessible surface area (ASA) using preferential interaction coefficients and the local-bulk domain model
    • Courtenay, E. S., Capp, M. W., Saecker, R. M., and Record, M. T., Jr. (2000) Thermodynamic analysis of interactions between denaturants and protein surface exposed on unfolding: interpretation of urea and guanidinium chloride m-values and their correlation with changes in accessible surface area (ASA) using preferential interaction coefficients and the local-bulk domain model, Proteins: Struct., Funct., Genet. 41 (S4), 72-85.
    • (2000) Proteins: Struct., Funct., Genet. , vol.41 , Issue.S4 , pp. 72-85
    • Courtenay, E.S.1    Capp, M.W.2    Saecker, R.M.3    Record Jr., M.T.4
  • 4
    • 0035176391 scopus 로고    scopus 로고
    • Thermodynamics of interactions of urea and guanidinium salts with protein surface: Relationship between solute effects on protein processes and changes in water-accessible surface area
    • Courtenay, E. S., Capp, M. W., and Record, M. T., Jr. (2001) Thermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface area, Protein Sci. 10, 2485-2497.
    • (2001) Protein Sci. , vol.10 , pp. 2485-2497
    • Courtenay, E.S.1    Capp, M.W.2    Record Jr., M.T.3
  • 5
    • 0027386592 scopus 로고
    • Betaine can eliminate the base pair composition dependence of DNA melting
    • Rees, W. A., Yager, T. D., Korte, J., and von Hippel, P. H. (1993) Betaine can eliminate the base pair composition dependence of DNA melting, Biochemistry 32, 137-144.
    • (1993) Biochemistry , vol.32 , pp. 137-144
    • Rees, W.A.1    Yager, T.D.2    Korte, J.3    Von Hippel, P.H.4
  • 6
    • 0024081225 scopus 로고
    • Conformation and thermostability of double-helical nucleic acids in aqueous solutions of urea
    • Babayan, Y. S. (1988) Conformation and thermostability of double-helical nucleic acids in aqueous solutions of urea, Mol. Biol. 22, 1204-1210.
    • (1988) Mol. Biol. , vol.22 , pp. 1204-1210
    • Babayan, Y.S.1
  • 7
    • 8744236141 scopus 로고
    • Conformation and thermal stability of DNA in aqueous urea solutions
    • Aslanyan, V. M., Babayan Y. S., and Arutyunyan, S. G. (1984) Conformation and thermal stability of DNA in aqueous urea solutions, Biophysics 29, 410-414.
    • (1984) Biophysics , vol.29 , pp. 410-414
    • Aslanyan, V.M.1    Babayan, Y.S.2    Arutyunyan, S.G.3
  • 8
    • 0017778968 scopus 로고
    • Calorimetric measurements of the transition enthalpy of DNA in aqueous urea solutions
    • Klump, H., and Burkart, W. (1977) Calorimetric measurements of the transition enthalpy of DNA in aqueous urea solutions, Biochim. Biophys. Acta 475, 601-604.
    • (1977) Biochim. Biophys. Acta , vol.475 , pp. 601-604
    • Klump, H.1    Burkart, W.2
  • 9
    • 0034641612 scopus 로고    scopus 로고
    • Mg2+-dependent compaction and folding of yeast tRNAPhe and the catalytic domain of the B. subtilis RNase P RNA determined by small-angle X-ray scattering
    • Fang, X., Littrell, K., Yang, X. J., Henderson, S. J., Siefert, S., Thiyagarajan, P., Pan, T., and Sosnick, T. R. (2000) Mg2+-dependent compaction and folding of yeast tRNAPhe and the catalytic domain of the B. subtilis RNase P RNA determined by small-angle X-ray scattering, Biochemistry 39 (36), 11107-11113.
    • (2000) Biochemistry , vol.39 , Issue.36 , pp. 11107-11113
    • Fang, X.1    Littrell, K.2    Yang, X.J.3    Henderson, S.J.4    Siefert, S.5    Thiyagarajan, P.6    Pan, T.7    Sosnick, T.R.8
  • 10
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. (1998) Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated, Adv. Protein Chem. 51, 355-432.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 11
    • 0141783830 scopus 로고    scopus 로고
    • Preferential interactions of urea with lysozyme and their linkage to protein denaturation
    • Timasheff, S. N., and Xie, G. (2003) Preferential interactions of urea with lysozyme and their linkage to protein denaturation, Biophys. Chem. 105, 421-448.
    • (2003) Biophys. Chem. , vol.105 , pp. 421-448
    • Timasheff, S.N.1    Xie, G.2
  • 13
    • 0034745484 scopus 로고    scopus 로고
    • Second virial coefficients as a measure of protein-osmolyte interactions
    • Weatherly, G. T., and Pielak, G. J. (2001) Second virial coefficients as a measure of protein-osmolyte interactions, Protein Sci. 10 (1), 12-16.
    • (2001) Protein Sci. , vol.10 , Issue.1 , pp. 12-16
    • Weatherly, G.T.1    Pielak, G.J.2
  • 14
    • 0029798239 scopus 로고    scopus 로고
    • Thermodynamic characterization of interactions of native bovine serum albumin with highly excluded (glycine betaine) and moderately accumulated (urea) solutes by a novel application of vapor pressure osmometry
    • Zhang, W., Capp, M. W., Bond, J. P., Anderson, C. F., and Record, M. T., Jr. (1996) Thermodynamic characterization of interactions of native bovine serum albumin with highly excluded (glycine betaine) and moderately accumulated (urea) solutes by a novel application of vapor pressure osmometry, Biochemistry 35, 10506-10516.
    • (1996) Biochemistry , vol.35 , pp. 10506-10516
    • Zhang, W.1    Capp, M.W.2    Bond, J.P.3    Anderson, C.F.4    Record Jr., M.T.5
  • 15
    • 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
  • 17
    • 0028962012 scopus 로고
    • Interpretation of preferential interaction coefficients of nonelectrolytes and of electrolyte ions in terms of a two-domain model
    • Record, M. T., Jr., and Anderson, C. F. (1995) Interpretation of preferential interaction coefficients of nonelectrolytes and of electrolyte ions in terms of a two-domain model, Biophys. J. 68, 786-794.
    • (1995) Biophys. J. , vol.68 , pp. 786-794
    • Record Jr., M.T.1    Anderson, C.F.2
  • 18
    • 0031776135 scopus 로고    scopus 로고
    • Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: A practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts
    • Record, M. T., Jr., Zhang, W., and Anderson, C. F. (1998) Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts, Adv. Protein Chem. 51, 281-353.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 281-353
    • Record Jr., M.T.1    Zhang, W.2    Anderson, C.F.3
  • 19
    • 0141448970 scopus 로고    scopus 로고
    • Preferential interactions in aqueous solutions of urea and KCl
    • Hong, J., Capp, M. W., Anderson, C. F., and Record, M. T. (2003) Preferential interactions in aqueous solutions of urea and KCl, Biophys. Chem. 105 (2-3), 517-532.
    • (2003) Biophys. Chem. , vol.105 , Issue.2-3 , pp. 517-532
    • Hong, J.1    Capp, M.W.2    Anderson, C.F.3    Record, M.T.4
  • 20
    • 67650040559 scopus 로고
    • Linked functions and reciprocal effects in hemoglobin: A second look
    • Wyman, J. (1964) Linked functions and reciprocal effects in hemoglobin: a second look, Adv. Protein Chem. 19, 223-286.
    • (1964) Adv. Protein Chem. , vol.19 , pp. 223-286
    • Wyman, J.1
  • 21
    • 33947475049 scopus 로고
    • Activity coefficients in aqueous solutions of sucrose, mannitol and their mixtures at 25°C
    • Robinson, R. A., and Stokes, R. H. (1961) Activity coefficients in aqueous solutions of sucrose, mannitol and their mixtures at 25°C, J. Phys. Chem. 65 (11), 1954-1958.
    • (1961) J. Phys. Chem. , vol.65 , Issue.11 , pp. 1954-1958
    • Robinson, R.A.1    Stokes, R.H.2
  • 22
    • 0001373502 scopus 로고
    • The thermodynamics of the ternary system: Urea-sodium chloride-water at 25°C
    • Bower, V. E., and Robinson, R. A. (1963) The thermodynamics of the ternary system: urea-sodium chloride-water at 25°C, J. Phys. Chem. 67, 1524-1527.
    • (1963) J. Phys. Chem. , vol.67 , pp. 1524-1527
    • Bower, V.E.1    Robinson, R.A.2
  • 23
    • 0025297716 scopus 로고
    • Large-scale preparation of mononucleosomal DNA from calf thymus for biophysical studies
    • Wang, L., Ferrari, M., and Bloomfield, V. A. (1990) Large-scale preparation of mononucleosomal DNA from calf thymus for biophysical studies, BioTechniques 9, 24-27.
    • (1990) BioTechniques , vol.9 , pp. 24-27
    • Wang, L.1    Ferrari, M.2    Bloomfield, V.A.3
  • 24
    • 0030917624 scopus 로고    scopus 로고
    • Binding of cationic (+4) alanine- And glycine-containing oligopeptides to double-stranded DNA: Thermodynamic analysis of effects of Coulombic interactions and alpha-helix induction
    • Padmanabhan, S., Zhang, W., Capp, M. W., Anderson, C. F., and Record, M. T., Jr. (1997) Binding of cationic (+4) alanine- and glycine-containing oligopeptides to double-stranded DNA: thermodynamic analysis of effects of Coulombic interactions and alpha-helix induction, Biochemistry 36 (17), 5193-5206.
    • (1997) Biochemistry , vol.36 , Issue.17 , pp. 5193-5206
    • Padmanabhan, S.1    Zhang, W.2    Capp, M.W.3    Anderson, C.F.4    Record Jr., M.T.5
  • 25
    • 0028945483 scopus 로고
    • Importance of Coulombic end effects on cation accumulation near oligoelectrolyte B-DNA: A demonstration using 23Na NMR
    • Stein, V. M., Bond, J. P., Capp, M. W., Anderson, C. F., and Record, M. T., Jr. (1995) Importance of Coulombic end effects on cation accumulation near oligoelectrolyte B-DNA: a demonstration using 23Na NMR, Biophys. J. 68 (3), 1063-1072.
    • (1995) Biophys. J. , vol.68 , Issue.3 , pp. 1063-1072
    • Stein, V.M.1    Bond, J.P.2    Capp, M.W.3    Anderson, C.F.4    Record Jr., M.T.5
  • 27
    • 0001201675 scopus 로고
    • The relationship between the Poisson-Boltzmann model and the condensation hypothesis: An analysis based on the low salt form of the donnan coefficient
    • Anderson, C. F., Record, M. T., Jr. (1980) The relationship between the Poisson-Boltzmann model and the condensation hypothesis: an analysis based on the low salt form of the donnan coefficient, Biophys. Chem. 11, 353-360.
    • (1980) Biophys. Chem. , vol.11 , pp. 353-360
    • Anderson, C.F.1    Record Jr., M.T.2
  • 28
    • 11644276439 scopus 로고
    • Limiting Laws and Counterion Condensation in Polyelectrolyte Solutions I. Colligative Properties
    • Manning, G. S. (1969) Limiting Laws and Counterion Condensation in Polyelectrolyte Solutions I. Colligative Properties, J. Chem. Phys. 51, 924-933.
    • (1969) J. Chem. Phys. , vol.51 , pp. 924-933
    • Manning, G.S.1
  • 31
    • 0014231119 scopus 로고
    • Deoxyribonucleate solutions: Sedimentation in a density gradient, partial specific volumes, density and refractive index increments, and preferential interactions
    • Cohen, G., and Eisenberg, H. (1968) Deoxyribonucleate solutions: sedimentation in a density gradient, partial specific volumes, density and refractive index increments, and preferential interactions, Biopolymers 6, 1077-1100.
    • (1968) Biopolymers , vol.6 , pp. 1077-1100
    • Cohen, G.1    Eisenberg, H.2
  • 32
    • 0016409155 scopus 로고
    • The interaction of actinomycin C3 and actinomine with DNA. A small-angle X-ray scattering study
    • Zipper, P., and Bünemann, H. (1975) The interaction of actinomycin C3 and actinomine with DNA. A small-angle X-ray scattering study, Eur. J. Biochem. 51, 3-17.
    • (1975) Eur. J. Biochem. , vol.51 , pp. 3-17
    • Zipper, P.1    Bünemann, H.2
  • 33
    • 84984085423 scopus 로고
    • Volume changes accompanying the thermal denaturation of deoxyribonucleic acid. I. Denaturation at neutral pH
    • Chapman, R. E., Jr., and Sturtevant, J. M. (1969) Volume changes accompanying the thermal denaturation of deoxyribonucleic acid. I. Denaturation at neutral pH, Biopolymers 7, 527-537.
    • (1969) Biopolymers , vol.7 , pp. 527-537
    • Chapman Jr., R.E.1    Sturtevant, J.M.2
  • 34
    • 8744220522 scopus 로고
    • The specific volume of various cationic forms of deoxyribonucleic acid
    • Hearst, J. E. (1962) The specific volume of various cationic forms of deoxyribonucleic acid, J. Mol. Biol. 4, 415-417.
    • (1962) J. Mol. Biol. , vol.4 , pp. 415-417
    • Hearst, J.E.1
  • 36
    • 0020790862 scopus 로고
    • Preferential interactions of proteins with solvent components in aqueous amino acid solutions
    • Arakawa, T., and Timasheff, S. N. (1983) Preferential interactions of proteins with solvent components in aqueous amino acid solutions, Arch. Biochem. Biophys. 224, 169-177.
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 169-177
    • Arakawa, T.1    Timasheff, S.N.2
  • 37
    • 0001449507 scopus 로고
    • Apparent molecular volumes of urea in several solvents as functions of temperature and concentration
    • Hamilton, D., and Stokes, R. H. (1972) Apparent molecular volumes of urea in several solvents as functions of temperature and concentration, J. Solution Chem. 1, 213-221.
    • (1972) J. Solution Chem. , vol.1 , pp. 213-221
    • Hamilton, D.1    Stokes, R.H.2
  • 38
    • 0345693568 scopus 로고
    • The apparent molal volume and adiabiatic compressibility of some organic solutes in water at 25°C
    • Lo Surdo, A., Shin, C., and Millero, F. J. (1978) The apparent molal volume and adiabiatic compressibility of some organic solutes in water at 25°C, Chem. Eng. Data 23, 197-201.
    • (1978) Chem. Eng. Data , vol.23 , pp. 197-201
    • Lo Surdo, A.1    Shin, C.2    Millero, F.J.3
  • 41
    • 0002558701 scopus 로고
    • Thermodynamic properties of solutions of amino acids and related substances. V. The activities of some hydroxy- And N-methylamino acids and proline in aqueous solution at twenty-five degrees
    • Smith, P. K., and Smith, E. R. B. (1940) Thermodynamic properties of solutions of amino acids and related substances. V. The activities of some hydroxy- and N-methylamino acids and proline in aqueous solution at twenty-five degrees, J. Biol. Chem. 132, 57-64.
    • (1940) J. Biol. Chem. , vol.132 , pp. 57-64
    • Smith, P.K.1    Smith, E.R.B.2
  • 42
    • 0001479267 scopus 로고
    • Isotonic solutions. I. The chemical potential of water in aqueous solutions of sodium chloride, potassium chloride, sulfuric acid, sucrose, urea, and glycerol at 25°C
    • Scatchard, G., Hamer, W. J., and Wood, S. E. (1938) Isotonic solutions. I. The chemical potential of water in aqueous solutions of sodium chloride, potassium chloride, sulfuric acid, sucrose, urea, and glycerol at 25°C, J. Am. Chem. Soc. 60, 3061-3070.
    • (1938) J. Am. Chem. Soc. , vol.60 , pp. 3061-3070
    • Scatchard, G.1    Hamer, W.J.2    Wood, S.E.3
  • 44
    • 0033614819 scopus 로고    scopus 로고
    • Enthalpy and heat capacity changes for formation of an oligomeric DNA duplex: Interpretation in terms of coupled processes of formation and association of single-stranded helices
    • Holbrook, J. A., Capp, M. W., Saecker, R. M., and Record, M. T., Jr. (1999) Enthalpy and heat capacity changes for formation of an oligomeric DNA duplex: interpretation in terms of coupled processes of formation and association of single-stranded helices, Biochemistry 38 (26), 8409-8422.
    • (1999) Biochemistry , vol.38 , Issue.26 , pp. 8409-8422
    • Holbrook, J.A.1    Capp, M.W.2    Saecker, R.M.3    Record Jr., M.T.4
  • 45
    • 0021755764 scopus 로고
    • Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect
    • Richmond, T. J. (1984) Solvent accessible surface area and excluded volume in proteins. Analytical equations for overlapping spheres and implications for the hydrophobic effect, J. Mol. Biol. 178, 63-89.
    • (1984) J. Mol. Biol. , vol.178 , pp. 63-89
    • Richmond, T.J.1
  • 46
    • 0031755274 scopus 로고    scopus 로고
    • Hydration of the phosphate group in double-helical DNA
    • Schneider, B., Patel, K., and Berman, H. M. (1998) Hydration of the phosphate group in double-helical DNA, Biophys. J. 75, 2422-2434.
    • (1998) Biophys. J. , vol.75 , pp. 2422-2434
    • Schneider, B.1    Patel, K.2    Berman, H.M.3
  • 47
    • 0027993455 scopus 로고
    • Hydration and partial compressibility of biological compounds
    • Chalikian, T. V., Sarvazyan, A. P., and Breslauer, K. J. (1994) Hydration and partial compressibility of biological compounds, Biophys. Chem. 51 (2-3), 89-107.
    • (1994) Biophys. Chem. , vol.51 , Issue.2-3 , pp. 89-107
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 48
    • 0025030410 scopus 로고
    • A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures
    • Schellman, J. A. (1990) A simple model for solvation in mixed solvents. Applications to the stabilization and destabilization of macromolecular structures, Biophys. Chem. 37 (1-3), 121-140.
    • (1990) Biophys. Chem. , vol.37 , Issue.1-3 , pp. 121-140
    • Schellman, J.A.1
  • 49
    • 0038311869 scopus 로고    scopus 로고
    • Protein stability in mixed solvents: A balance of contact interaction and excluded volume
    • Schellman, J. A. (2003) Protein stability in mixed solvents: a balance of contact interaction and excluded volume, Biophys. J. 85 (1), 108-125.
    • (2003) Biophys. J. , vol.85 , Issue.1 , pp. 108-125
    • Schellman, J.A.1
  • 50
    • 0037123063 scopus 로고    scopus 로고
    • Thermodynamic Expressions Relating Different Types of Preferential Interaction Coefficients in Solutions Containing Two Solute Components
    • Anderson, C. F., Courtenay, E. S., and Record, M. T., Jr. (2002) Thermodynamic Expressions Relating Different Types of Preferential Interaction Coefficients in Solutions Containing Two Solute Components, J. Phys. Chem. B 106, 418-433.
    • (2002) J. Phys. Chem. B , vol.106 , pp. 418-433
    • Anderson, C.F.1    Courtenay, E.S.2    Record Jr., M.T.3
  • 52
    • 0037059028 scopus 로고    scopus 로고
    • Generalized derivation of an exact relationship linking different coefficients that characterize thermodynamic effects of preferential interactions
    • Anderson, C. F., Felitsky, D., Hong, J., and Record, M. T., Jr. (2002) Generalized derivation of an exact relationship linking different coefficients that characterize thermodynamic effects of preferential interactions, Biophys. Chem. 101, 493-507.
    • (2002) Biophys. Chem. , vol.101 , pp. 493-507
    • Anderson, C.F.1    Felitsky, D.2    Hong, J.3    Record Jr., M.T.4
  • 53
    • 0028222102 scopus 로고
    • Influence of base composition, base sequence, and duplex structure on DNA hydration: Apparent molar volumes and apparent molar adiabatic compressibilities of synthetic and natural DNA duplexes at 25°C
    • Chalikian, T. V., Sarvazyan, A. P., Plum, G. E., and Breslauer, K. J. (1994) Influence of base composition, base sequence, and duplex structure on DNA hydration: apparent molar volumes and apparent molar adiabatic compressibilities of synthetic and natural DNA duplexes at 25°C, Biochemistry 33 (9), 2394-2401.
    • (1994) Biochemistry , vol.33 , Issue.9 , pp. 2394-2401
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Plum, G.E.3    Breslauer, K.J.4
  • 54
    • 0001306360 scopus 로고
    • Anomalous heat capacity of hydrophobic solvation
    • Gill, S. J., Dec, S. F., Olofsson, G., and Wadsoe, I. (1985) Anomalous heat capacity of hydrophobic solvation, J. Phys. Chem. 89 (17), 3758-3761.
    • (1985) J. Phys. Chem. , vol.89 , Issue.17 , pp. 3758-3761
    • Gill, S.J.1    Dec, S.F.2    Olofsson, G.3    Wadsoe, I.4
  • 56
    • 0014271642 scopus 로고
    • Heats of the helix-coil transitions of the poly A-poly U complexes
    • Krakauer, H., and Sturtevant, J. M. (1968) Heats of the helix-coil transitions of the poly A-poly U complexes, Biopolymers 6 (4), 491-512.
    • (1968) Biopolymers , vol.6 , Issue.4 , pp. 491-512
    • Krakauer, H.1    Sturtevant, J.M.2
  • 57
    • 84984087761 scopus 로고
    • Determination of stability of the DNA double helix in an aqueous medium
    • Privalov, P. L., Ptitsyn, O. B., and Birshtein, T. M. (1969) Determination of stability of the DNA double helix in an aqueous medium, Biopolymers 8, 559-571.
    • (1969) Biopolymers , vol.8 , pp. 559-571
    • Privalov, P.L.1    Ptitsyn, O.B.2    Birshtein, T.M.3
  • 58
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: The roles of ion association or release, screening, and ion effects on water activity
    • Record, M. T., Jr., Anderson, C. F., and Lohman, T. M. (1978) Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity, Q. Rev.Biophys. 11 (2), 103-178.
    • (1978) Q. Rev.Biophys. , vol.11 , Issue.2 , pp. 103-178
    • Record Jr., M.T.1    Anderson, C.F.2    Lohman, T.M.3
  • 60
    • 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
  • 61
    • 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
  • 62
    • 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
  • 63
    • 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
  • 64
    • 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
  • 65
    • 0032080534 scopus 로고    scopus 로고
    • Urea effects on protein stability: Hydrogen bonding and the hydrophobic effect
    • Zou, Q., Habermann-Rottinghaus, S. M., and Murphy, K. P. (1998) Urea effects on protein stability: hydrogen bonding and the hydrophobic effect, Proteins 31, 107-115.
    • (1998) Proteins , vol.31 , pp. 107-115
    • Zou, Q.1    Habermann-Rottinghaus, S.M.2    Murphy, K.P.3
  • 66
    • 8744225646 scopus 로고    scopus 로고
    • The Exclusion of Glycine Betaine from Anionic Biopolymer Surface: Why Glycine Betaine Is an Effective Osmoprotectant but Also a Compatible Solute
    • Felitsky, D. J., Cannon, J. G., Capp, M. W. Hong, J., VanWynsberghe, A. W., Anderson, C. F., and Record, M. T., Jr. (2004) The Exclusion of Glycine Betaine from Anionic Biopolymer Surface: Why Glycine Betaine Is an Effective Osmoprotectant but Also a Compatible Solute, Biochemistry 43, 14732-14743..
    • (2004) Biochemistry , vol.43 , pp. 14732-14743
    • Felitsky, D.J.1    Cannon, J.G.2    Capp, M.W.3    Hong, J.4    VanWynsberghe, A.W.5    Anderson, C.F.6    Record Jr., M.T.7
  • 67
    • 3142655877 scopus 로고    scopus 로고
    • Application of the local-bulk partitioning and competitive binding models to interpret preferential interactions of glycine betaine and urea with protein surface
    • Felitsky, D. J., and Record, M. T., Jr. (2004) Application of the local-bulk partitioning and competitive binding models to interpret preferential interactions of glycine betaine and urea with protein surface, Biochemistry 43 (28) 9276-9288.
    • (2004) Biochemistry , vol.43 , Issue.28 , pp. 9276-9288
    • Felitsky, D.J.1    Record Jr., M.T.2
  • 68
    • 0033592945 scopus 로고    scopus 로고
    • Applicability of urea in the thermodynamic analysis of secondary and tertiary RNA folding
    • Shelton, V. M., Sosnick, T. R., and Pan, T. (1999) Applicability of urea in the thermodynamic analysis of secondary and tertiary RNA folding. Biochemistry 38, 16831-16839.
    • (1999) Biochemistry , vol.38 , pp. 16831-16839
    • Shelton, V.M.1    Sosnick, T.R.2    Pan, T.3


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