메뉴 건너뛰기




Volumn 1478, Issue 2, 2000, Pages 309-317

Calorimetric evidence for a native-like conformation of hen egg-white lysozyme dissolved in glycerol

Author keywords

Conformational stability; Glycerol; Lysozyme; Molten globule

Indexed keywords

GLYCEROL; LYSOZYME; WATER;

EID: 0034704986     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(00)00028-5     Document Type: Article
Times cited : (33)

References (63)
  • 2
    • 0342542086 scopus 로고
    • The Royal Society of Chemistry, London
    • F. Franks, Water, The Royal Society of Chemistry, London, 1993.
    • (1993) Water
    • Franks, F.1
  • 3
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • Kuntz I.D., Kauzmann W. Jr. Hydration of proteins and polypeptides. Adv. Protein Chem. 28:1974;239-345.
    • (1974) Adv. Protein Chem. , vol.28 , pp. 239-345
    • Kuntz, I.D.1    Kauzmann W., Jr.2
  • 4
    • 0015210126 scopus 로고
    • Solvophobic interactions and micelle formation in structure forming nonaqueous solvents
    • Ray A. Solvophobic interactions and micelle formation in structure forming nonaqueous solvents. Nature. 231:1971;313-315.
    • (1971) Nature , vol.231 , pp. 313-315
    • Ray, A.1
  • 5
    • 0029902287 scopus 로고    scopus 로고
    • On protein denaturation in aqueous-organic mixtures but not in pure organic solvents
    • Griebenow K., Klibanov A.M. On protein denaturation in aqueous-organic mixtures but not in pure organic solvents. J. Am. Chem. Soc. 118:1996;11695-11700.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11695-11700
    • Griebenow, K.1    Klibanov, A.M.2
  • 8
    • 0033586348 scopus 로고    scopus 로고
    • Protein refolding in predominantly organic media markedly enhanced by common salts
    • Rariy R.V., Klibanov A.M. Protein refolding in predominantly organic media markedly enhanced by common salts. Biotechnol. Bioeng. 62:1999;704-710.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 704-710
    • Rariy, R.V.1    Klibanov, A.M.2
  • 9
    • 0033573999 scopus 로고    scopus 로고
    • Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol
    • Knubovets T., Osterhout J.J., Connolly P.J., Klibanov A.M. Structure, thermostability, and conformational flexibility of hen egg-white lysozyme dissolved in glycerol. Proc. Natl. Acad. Sci. USA. 96:1999;1262-1267.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1262-1267
    • Knubovets, T.1    Osterhout, J.J.2    Connolly, P.J.3    Klibanov, A.M.4
  • 10
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4:1995;2411-2423.
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 11
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov P.L., Potekhin S.A. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol. 131:1986;4-51.
    • (1986) Methods Enzymol. , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 12
    • 0018588511 scopus 로고
    • Stability of proteins: Small globular proteins
    • Privalov P.L. Stability of proteins: small globular proteins. Adv. Protein Chem. 33:1979;167-241.
    • (1979) Adv. Protein Chem. , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 13
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin
    • Sanchez-Ruiz J.M., Lopez-Lacomba J.L., Cortijo M., Mateo P.L. Differential scanning calorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry. 27:1988;1648-1652.
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanchez-Ruiz, J.M.1    Lopez-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 14
  • 15
    • 0001826608 scopus 로고
    • Biological thermodynamic data for the calibration of differential scanning calorimeters: Heat capacity data on the unfolding transition of lysozyme in solution
    • Schwarz F.P. Biological thermodynamic data for the calibration of differential scanning calorimeters: heat capacity data on the unfolding transition of lysozyme in solution. Thermochim. Acta. 147:1989;71-91.
    • (1989) Thermochim. Acta , vol.147 , pp. 71-91
    • Schwarz, F.P.1
  • 16
    • 0028845120 scopus 로고
    • Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution
    • Privalov G., Kavina V., Freire E., Privalov P.L. Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution. Anal. Biochem. 232:1995;79-85.
    • (1995) Anal. Biochem. , vol.232 , pp. 79-85
    • Privalov, G.1    Kavina, V.2    Freire, E.3    Privalov, P.L.4
  • 17
    • 0000206582 scopus 로고    scopus 로고
    • Selective catalytic oxidation with air of glycerol and oxygenated derivatives on platinum metals
    • Fordham P., Garcia R., Besson M., Gallezot P. Selective catalytic oxidation with air of glycerol and oxygenated derivatives on platinum metals. Stud. Surf. Sci. Catal. 101:1996;161-170.
    • (1996) Stud. Surf. Sci. Catal. , vol.101 , pp. 161-170
    • Fordham, P.1    Garcia, R.2    Besson, M.3    Gallezot, P.4
  • 18
    • 0024653016 scopus 로고
    • Enzymatic catalysis in anhydrous organic solvents
    • Klibanov A.M. Enzymatic catalysis in anhydrous organic solvents. Trends Biochem. Sci. 14:1989;141-144.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 141-144
    • Klibanov, A.M.1
  • 19
    • 0017225714 scopus 로고
    • Thermodynamic investigations of proteins. III. Thermodynamic description of lysozyme
    • Pfeil W., Privalov P.L. Thermodynamic investigations of proteins. III. Thermodynamic description of lysozyme. Biophys. Chem. 4:1976;41-50.
    • (1976) Biophys. Chem. , vol.4 , pp. 41-50
    • Pfeil, W.1    Privalov, P.L.2
  • 20
    • 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
  • 22
    • 0028966781 scopus 로고
    • Modeling protein stability as heteropolymer collapse
    • Dill K.A., Stigter D. Modeling protein stability as heteropolymer collapse. Adv. Protein Chem. 46:1995;59-104.
    • (1995) Adv. Protein Chem. , vol.46 , pp. 59-104
    • Dill, K.A.1    Stigter, D.2
  • 23
    • 0028929583 scopus 로고
    • Free energy balance in protein folding
    • Honig B., Yang A.S. Free energy balance in protein folding. Adv. Protein Chem. 46:1995;27-58.
    • (1995) Adv. Protein Chem. , vol.46 , pp. 27-58
    • Honig, B.1    Yang, A.S.2
  • 24
    • 0029886627 scopus 로고    scopus 로고
    • How molten is the molten globule?
    • Ptitsyn O. How molten is the molten globule? Nat. Struct. Biol. 3:1996;488-490.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 488-490
    • Ptitsyn, O.1
  • 25
    • 0029040449 scopus 로고
    • Thermodynamic stability of the molten globule states of apomyoglobin
    • Nishii I., Kataoka M., Goto Y. Thermodynamic stability of the molten globule states of apomyoglobin. J. Mol. Biol. 250:1995;223-238.
    • (1995) J. Mol. Biol. , vol.250 , pp. 223-238
    • Nishii, I.1    Kataoka, M.2    Goto, Y.3
  • 26
    • 0028143596 scopus 로고
    • Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry
    • Hamada D., Kidokoro S., Fukada H., Takahashi K., Goto Y. Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc. Natl. Acad. Sci. USA. 91:1994;10325-10329.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10325-10329
    • Hamada, D.1    Kidokoro, S.2    Fukada, H.3    Takahashi, K.4    Goto, Y.5
  • 27
    • 0028346251 scopus 로고
    • Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride
    • Hagihara Y., Tan Y., Goto Y. Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride. J. Mol. Biol. 237:1994;336-348.
    • (1994) J. Mol. Biol. , vol.237 , pp. 336-348
    • Hagihara, Y.1    Tan, Y.2    Goto, Y.3
  • 28
    • 0030701981 scopus 로고    scopus 로고
    • Effects of organic solvents on protein structures observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide
    • Bhattacharjya S., Balaram P. Effects of organic solvents on protein structures observation of a structured helical core in hen egg-white lysozyme in aqueous dimethylsulfoxide. Proteins. 29:1997;492-507.
    • (1997) Proteins , vol.29 , pp. 492-507
    • Bhattacharjya, S.1    Balaram, P.2
  • 29
    • 0030894810 scopus 로고    scopus 로고
    • Hexafluoroacetone hydrate as a structure modifier in proteins: Characterization of a molten globule state of hen egg-white lysozyme
    • Bhattacharjya S., Balaram P. Hexafluoroacetone hydrate as a structure modifier in proteins: characterization of a molten globule state of hen egg-white lysozyme. Protein Sci. 6:1997;1065-1073.
    • (1997) Protein Sci. , vol.6 , pp. 1065-1073
    • Bhattacharjya, S.1    Balaram, P.2
  • 31
    • 0032754813 scopus 로고    scopus 로고
    • Polyol-induced molten globule of cytochrome c: An evidence for stabilization by hydrophobic interaction
    • Kamiyama T., Sadahide Y., Nogusa Y., Gekko K. Polyol-induced molten globule of cytochrome c: an evidence for stabilization by hydrophobic interaction. Biochim. Biophys. Acta. 1434:1999;44-57.
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 44-57
    • Kamiyama, T.1    Sadahide, Y.2    Nogusa, Y.3    Gekko, K.4
  • 32
    • 0027080869 scopus 로고
    • Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation
    • Lepock J.R., Ritchie K.P., Kolios M.C., Rodahl A.M., Heinz K.A., Kruuv J. Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry. 31:1992;12706-12712.
    • (1992) Biochemistry , vol.31 , pp. 12706-12712
    • Lepock, J.R.1    Ritchie, K.P.2    Kolios, M.C.3    Rodahl, A.M.4    Heinz, K.A.5    Kruuv, J.6
  • 33
    • 0022423885 scopus 로고
    • Comparison of the transient folding intermediates in lysozyme and α-lactalbumin
    • Kuwajima K., Hiraoka Y., Ikeguchi M., Sugai S. Comparison of the transient folding intermediates in lysozyme and α-lactalbumin. Biochemistry. 24:1985;874-881.
    • (1985) Biochemistry , vol.24 , pp. 874-881
    • Kuwajima, K.1    Hiraoka, Y.2    Ikeguchi, M.3    Sugai, S.4
  • 34
    • 0026013162 scopus 로고
    • Demonstration by NMR of folding domains in lysozyme
    • Miranker A., Radford S.E., Karplus M., Dobson C.M. Demonstration by NMR of folding domains in lysozyme. Nature. 349:1991;633-636.
    • (1991) Nature , vol.349 , pp. 633-636
    • Miranker, A.1    Radford, S.E.2    Karplus, M.3    Dobson, C.M.4
  • 35
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford S.E., Dobson C.M., Evans P.A. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature. 358:1992;302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 37
    • 0026630480 scopus 로고
    • Simulation of the thermal denaturation of hen egg white lysozyme trapping the molten globule state
    • Mark A.E., vanGunsteren W.F. Simulation of the thermal denaturation of hen egg white lysozyme trapping the molten globule state. Biochemistry. 31:1992;7745-7748.
    • (1992) Biochemistry , vol.31 , pp. 7745-7748
    • Mark, A.E.1    Vangunsteren, W.F.2
  • 38
  • 39
    • 0001919558 scopus 로고
    • Preferential interactions of water and cosolvents with proteins
    • in: R.B. Gregory (Ed.), Marcel Dekker, New York
    • S.N. Timasheff, Preferential interactions of water and cosolvents with proteins, in: R.B. Gregory (Ed.), Protein-Solvent Interactions, Marcel Dekker, New York, 1995, pp. 445-482.
    • (1995) Protein-Solvent Interactions , pp. 445-482
    • Timasheff, S.N.1
  • 40
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff S.N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51:1998;355-432.
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 42
    • 0027484016 scopus 로고
    • Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation
    • Thomas P.D., Dill K.A. Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation. Protein Sci. 2:1993;2050-2065.
    • (1993) Protein Sci. , vol.2 , pp. 2050-2065
    • Thomas, P.D.1    Dill, K.A.2
  • 43
    • 0033586734 scopus 로고    scopus 로고
    • Structure of lysozyme dissolved in neat organic solvents as assessed by NMR and CD spectroscopies
    • Knubovets T., Osterhout J.J., Klibanov A.M. Structure of lysozyme dissolved in neat organic solvents as assessed by NMR and CD spectroscopies. Biotechnol. Bioeng. 63:1999;242-248.
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 242-248
    • Knubovets, T.1    Osterhout, J.J.2    Klibanov, A.M.3
  • 44
    • 0030567341 scopus 로고    scopus 로고
    • Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol
    • Cammers-Goodwin A., Allen T.J., Oslick S.L., McClure K.F., Lee J.H., Kemp D.S. Mechanism of stabilization of helical conformations of polypeptides by water containing trifluoroethanol. J. Am. Chem. Soc. 118:1996;3082-3090.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3082-3090
    • Cammers-Goodwin, A.1    Allen, T.J.2    Oslick, S.L.3    McClure, K.F.4    Lee, J.H.5    Kemp, D.S.6
  • 45
    • 0032514771 scopus 로고    scopus 로고
    • Trifluoroethanol promotes helix formation by destabilizing backbone exposure desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding
    • Kentsis A., Sosnick T.R. Trifluoroethanol promotes helix formation by destabilizing backbone exposure desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding. Biochemistry. 37:1998;14613-14622.
    • (1998) Biochemistry , vol.37 , pp. 14613-14622
    • Kentsis, A.1    Sosnick, T.R.2
  • 46
    • 0032894467 scopus 로고    scopus 로고
    • Molecular simulation of the effects of alcohols on peptide structure
    • Dwyer D.S. Molecular simulation of the effects of alcohols on peptide structure. Biopolymers. 49:1999;635-645.
    • (1999) Biopolymers , vol.49 , pp. 635-645
    • Dwyer, D.S.1
  • 47
    • 0027160575 scopus 로고
    • Structural energetics of the molten globule state
    • Haynie D.T., Freire E. Structural energetics of the molten globule state. Proteins Struct. Funct. Genet. 16:1993;115-140.
    • (1993) Proteins Struct. Funct. Genet. , vol.16 , pp. 115-140
    • Haynie, D.T.1    Freire, E.2
  • 48
    • 0017583479 scopus 로고
    • Solvents, interfaces and protein structure
    • F.M. Richards and T. Richmond, Solvents, interfaces and protein structure, Ciba Found. Symp. (1977) 23-45.
    • (1977) Ciba Found. Symp. , pp. 23-45
    • Richards, F.M.1    Richmond, T.2
  • 49
  • 50
    • 0030590219 scopus 로고    scopus 로고
    • Interactions between a helical residue and tertiary structures: Helix propensities in small peptides and in native proteins
    • Qian H., Chan S.I. Interactions between a helical residue and tertiary structures: helix propensities in small peptides and in native proteins. J. Mol. Biol. 261:1996;279-288.
    • (1996) J. Mol. Biol. , vol.261 , pp. 279-288
    • Qian, H.1    Chan, S.I.2
  • 51
    • 0026839336 scopus 로고    scopus 로고
    • Quantitative theory of the globule-to-coil transition. 1. Link density distribution in a globule and its radius of gyration
    • Grosberg A.Yu., Kuznetsov D.V. Quantitative theory of the globule-to-coil transition. 1. Link density distribution in a globule and its radius of gyration. Macromolecules. 25:1999;1970-1979.
    • (1999) Macromolecules , vol.25 , pp. 1970-1979
    • Grosberg, A.Yu.1    Kuznetsov, D.V.2
  • 52
    • 0019872612 scopus 로고
    • Thermodynamic and kinetic examination of protein stabilization by glycerol
    • Gekko K., Timasheff S.N. Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry. 20:1981;4677-4686.
    • (1981) Biochemistry , vol.20 , pp. 4677-4686
    • Gekko, K.1    Timasheff, S.N.2
  • 53
    • 0019590230 scopus 로고
    • Thermodynamics of polyol-induced thermal stabilization of chymotrypsinogen
    • Gekko K., Morikawa T. Thermodynamics of polyol-induced thermal stabilization of chymotrypsinogen. J. Biochem. (Tokyo). 90:1981;51-60.
    • (1981) J. Biochem. (Tokyo) , vol.90 , pp. 51-60
    • Gekko, K.1    Morikawa, T.2
  • 54
    • 0020123955 scopus 로고
    • Calorimetric study on thermal denaturation of lysozyme in polyol-water mixtures
    • Gekko K. Calorimetric study on thermal denaturation of lysozyme in polyol-water mixtures. J. Biochem. (Tokyo). 91:1982;1197-1204.
    • (1982) J. Biochem. (Tokyo) , vol.91 , pp. 1197-1204
    • Gekko, K.1
  • 55
    • 0006179834 scopus 로고    scopus 로고
    • Hydration changes upon protein unfolding cosolvent effect: Analysis
    • Hammou H.O., Plaza del Pino I.M., Sanchez-Ruiz J.M. Hydration changes upon protein unfolding cosolvent effect: analysis. New J. Chem. 22:1998;1453-1461.
    • (1998) New J. Chem. , vol.22 , pp. 1453-1461
    • Hammou, H.O.1    Plaza Del Pino, I.M.2    Sanchez-Ruiz, J.M.3
  • 56
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions
    • Nozaki Y., Tanford C. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. J. Biol. Chem. 246:1971;2211-2217.
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2
  • 57
    • 76549182497 scopus 로고
    • The solubility of amino acids and related compounds in aqueous ethylene glycol solutions
    • Nozaki Y., Tanford C. The solubility of amino acids and related compounds in aqueous ethylene glycol solutions. J. Biol. Chem. 240:1965;3658.
    • (1965) J. Biol. Chem. , vol.240 , pp. 3658
    • Nozaki, Y.1    Tanford, C.2
  • 58
    • 0019741203 scopus 로고
    • Mechanism of polyol-induced protein stabilization: Solubility of amino acids and diglycine in aqueous polyol solutions
    • Gekko K. Mechanism of polyol-induced protein stabilization: solubility of amino acids and diglycine in aqueous polyol solutions. J. Biochem. (Tokyo). 90:1981;1633-1641.
    • (1981) J. Biochem. (Tokyo) , vol.90 , pp. 1633-1641
    • Gekko, K.1
  • 59
    • 1542502033 scopus 로고    scopus 로고
    • Microcalorimetric study of the effect of dimethylsulfoxide on the heat denaturation of lysozyme
    • Kovrigin E.L., Potekhin S.A. Microcalorimetric study of the effect of dimethylsulfoxide on the heat denaturation of lysozyme. Biofizika (Moscow). 41:1996;1201-1206.
    • (1996) Biofizika (Moscow) , vol.41 , pp. 1201-1206
    • Kovrigin, E.L.1    Potekhin, S.A.2
  • 60
    • 0032506017 scopus 로고    scopus 로고
    • Limited internal friction in the rate-limiting step of a two-state protein folding reaction
    • Plaxco K.W., Baker D. Limited internal friction in the rate-limiting step of a two-state protein folding reaction. Proc. Natl. Acad. Sci. USA. 95:1998;13591-13596.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13591-13596
    • Plaxco, K.W.1    Baker, D.2
  • 61
    • 0033596697 scopus 로고    scopus 로고
    • Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil
    • Bhattacharyya R.P., Sosnick T.R. Viscosity dependence of the folding kinetics of a dimeric and monomeric coiled coil. Biochemistry. 38:1999;2601-2609.
    • (1999) Biochemistry , vol.38 , pp. 2601-2609
    • Bhattacharyya, R.P.1    Sosnick, T.R.2
  • 63
    • 0031555514 scopus 로고    scopus 로고
    • Correlation between catalytic activity and secondary structure of subtilisin dissolved in organic solvents
    • Xu K., Griebenow K., Klibanov A.M. Correlation between catalytic activity and secondary structure of subtilisin dissolved in organic solvents. Biotechnol. Bioeng. 56:1997;485-491.
    • (1997) Biotechnol. Bioeng. , vol.56 , pp. 485-491
    • Xu, K.1    Griebenow, K.2    Klibanov, A.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.