메뉴 건너뛰기




Volumn 39, Issue 3, 2007, Pages 187-196

Complexity of aromatic ring-flip motions in proteins: Y97 ring dynamics in cytochrome c observed by cross-relaxation suppressed exchange NMR spectroscopy

Author keywords

Arrhenius and non Arrhenius behavior; Cytochrome c; Exchange spectroscopy; Protein dynamics; Ring flip motion

Indexed keywords

CYTOCHROME C; GUANIDINE DERIVATIVE;

EID: 35448960711     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-007-9186-2     Document Type: Article
Times cited : (19)

References (61)
  • 3
    • 0000180763 scopus 로고
    • Temperature dependence of the hydrophobic interaction in protein folding
    • Baldwin RL (1986) Temperature dependence of the hydrophobic interaction in protein folding. Proc Natl Acad Sci USA 83:8069-8072
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8069-8072
    • Baldwin, R.L.1
  • 4
    • 0001221788 scopus 로고    scopus 로고
    • Existence of negative activation energies in simple bimolecular metathesis reactions and some observations on too fast reactions
    • Benson SW, Dobis O (1998) Existence of negative activation energies in simple bimolecular metathesis reactions and some observations on too fast reactions. J Phys Chem A 102:5175-5181
    • (1998) J Phys Chem A , vol.102 , pp. 5175-5181
    • Benson, S.W.1    Dobis, O.2
  • 5
    • 0037069399 scopus 로고    scopus 로고
    • Protein stabilization by urea and guanidine hydrochloride
    • Bhuyan AK (2002) Protein stabilization by urea and guanidine hydrochloride. Biochemistry 41:13386-13394
    • (2002) Biochemistry , vol.41 , pp. 13386-13394
    • Bhuyan, A.K.1
  • 6
    • 0024733407 scopus 로고
    • Intermdeiates and barrier crossing in a random energy model with applications to protein folding
    • Bryngelson JD, Wolynes PG (1989) Intermdeiates and barrier crossing in a random energy model with applications to protein folding. J Phys Chem 93:6902-6915
    • (1989) J Phys Chem , vol.93 , pp. 6902-6915
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 7
    • 0028947257 scopus 로고
    • Funnels, pathways and the energy landscape of protein folding: A synthesis
    • Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (1995) Funnels, pathways and the energy landscape of protein folding: A synthesis. Proteins 21:167-195
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 8
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell GW, Louie GV, Brayer GD (1990) High-resolution three-dimensional structure of horse heart cytochrome c. J Mol Biol 214:585-595
    • (1990) J Mol Biol , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 10
    • 0024977347 scopus 로고
    • Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations
    • Chan B-l, Baase WA, Schellman JA (1989) Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry 28:691-699
    • (1989) Biochemistry , vol.28 , pp. 691-699
    • Chan, B.-L.1    Baase, W.A.2    Schellman, J.A.3
  • 11
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA (1990) Dominant forces in protein folding. Biochemistry 29:7133-7155
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 12
    • 0025856806 scopus 로고
    • Denatured states of proteins
    • Dill KA, Shortle D (1991) Denatured states of proteins. Annu Rev Biochem 60:795-825
    • (1991) Annu Rev Biochem , vol.60 , pp. 795-825
    • Dill, K.A.1    Shortle, D.2
  • 13
    • 33845923185 scopus 로고    scopus 로고
    • The effects of cosolutes on protein dynamics: The reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide
    • Doan-Nguyen V, Loria JP (2007) The effects of cosolutes on protein dynamics: The reversal of denaturant-induced protein fluctuations by trimethylamine N-oxide. Protein Sci 16:20-29
    • (2007) Protein Sci , vol.16 , pp. 20-29
    • Doan-Nguyen, V.1    Loria, J.P.2
  • 14
    • 0029994817 scopus 로고    scopus 로고
    • Using buried water molecules to explore the energy landscape of proteins
    • Denisov VP, Peters J, Hörlein HD, Halle B (1996) Using buried water molecules to explore the energy landscape of proteins. Nat Struct Biol 3:505-509
    • (1996) Nat Struct Biol , vol.3 , pp. 505-509
    • Denisov, V.P.1    Peters, J.2    Hörlein, H.D.3    Halle, B.4
  • 15
    • 0030841382 scopus 로고    scopus 로고
    • The effects of denaturants on protein structure
    • Dunbar J, Yennawar HP, Banerjee S, Luo J et al (1997) The effects of denaturants on protein structure. Protein Sci 6:1272-1733
    • (1997) Protein Sci , vol.6 , pp. 1272-1733
    • Dunbar, J.1    Yennawar, H.P.2    Banerjee, S.3    Luo, J.4
  • 16
    • 0028352044 scopus 로고
    • Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands
    • Elöve GA, Bhuyan AK, Roder H (1994) Kinetic mechanism of cytochrome c folding: Involvement of the heme and its ligands. Biochemistry 33:6925-6935
    • (1994) Biochemistry , vol.33 , pp. 6925-6935
    • Elöve, G.A.1    Bhuyan, A.K.2    Roder, H.3
  • 17
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander SW, Mayne L (1992) Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR. Annu Rev Biophys Biomol Struct 21:243-265
    • (1992) Annu Rev Biophys Biomol Struct , vol.21 , pp. 243-265
    • Englander, S.W.1    Mayne, L.2
  • 20
    • 44949290550 scopus 로고
    • Quantitative evaluation of two-dimensional cross-relaxation NMR spectra of proteins. Interprotein distances in turkey ovomucoid third domain
    • Fejzo J, Zolnai Z, Macura S, Markley JL (1990) Quantitative evaluation of two-dimensional cross-relaxation NMR spectra of proteins. Interprotein distances in turkey ovomucoid third domain. J Magn Reson 88:93-110
    • (1990) J Magn Reson , vol.88 , pp. 93-110
    • Fejzo, J.1    Zolnai, Z.2    Macura, S.3    Markley, J.L.4
  • 21
    • 0002641301 scopus 로고
    • Strategies for eliminating unwanted cross-relaxation and coherence-transfer effects from two-dimensional chemical exchange spectra
    • Fejzo J, Westler WM, Macura S, Markley JL (1991) Strategies for eliminating unwanted cross-relaxation and coherence-transfer effects from two-dimensional chemical exchange spectra. J Magn Reson 92:20-29
    • (1991) J Magn Reson , vol.92 , pp. 20-29
    • Fejzo, J.1    Westler, W.M.2    Macura, S.3    Markley, J.L.4
  • 22
    • 5144223810 scopus 로고    scopus 로고
    • Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glass, control protein motions and fluctuations
    • Fenimore PW, Frauenfelder H, McMahon BH, Young RD (2004) Bulk-solvent and hydration-shell fluctuations, similar to alpha- and beta-fluctuations in glass, control protein motions and fluctuations. Proc Natl Acad Sci USA 101:14408-14413
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14408-14413
    • Fenimore, P.W.1    Frauenfelder, H.2    McMahon, B.H.3    Young, R.D.4
  • 23
    • 0003057754 scopus 로고
    • Protein dynamics by solid state NMR: Aromatic rings of the coat protein in fd bateriophage
    • Gall CM, Cross TA, DiVerdi JA, Opella SJ (1982) Protein dynamics by solid state NMR: Aromatic rings of the coat protein in fd bateriophage. Proc Natl Acad Sci USA 79:101-105
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 101-105
    • Gall, C.M.1    Cross, T.A.2    DiVerdi, J.A.3    Opella, S.J.4
  • 24
    • 3042720458 scopus 로고    scopus 로고
    • Sequence-dependent nucleotide dynamics revealed by intercalated ring rotation in DNA-bisnaphthalimide complexes
    • Gallego J (2004) Sequence-dependent nucleotide dynamics revealed by intercalated ring rotation in DNA-bisnaphthalimide complexes. Nucleic Acid Res 32:3607-3614
    • (2004) Nucleic Acid Res , vol.32 , pp. 3607-3614
    • Gallego, J.1
  • 25
    • 28444453002 scopus 로고    scopus 로고
    • Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data
    • Grishaev A, Wu J, Trewhella J, Bax A (2005) Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data. J Am Chem Soc 127:16621-16628
    • (2005) J Am Chem Soc , vol.127 , pp. 16621-16628
    • Grishaev, A.1    Wu, J.2    Trewhella, J.3    Bax, A.4
  • 26
    • 9344263447 scopus 로고    scopus 로고
    • Infrequent cavity-forming fluctuations in HPr from Staphylococcus carnosus revealed by pressure- and temperature-dependent tyrosine ring flips
    • Hattori M, Li H, Yamada H, Akasaka K et al (2004) Infrequent cavity-forming fluctuations in HPr from Staphylococcus carnosus revealed by pressure- and temperature-dependent tyrosine ring flips. Protein Sci 13:3104-3114
    • (2004) Protein Sci , vol.13 , pp. 3104-3114
    • Hattori, M.1    Li, H.2    Yamada, H.3    Akasaka, K.4
  • 27
    • 0022555887 scopus 로고
    • Internal dynamics of proteins
    • Karplus M (1986) Internal dynamics of proteins. Methods Enzymol 131:283-307
    • (1986) Methods Enzymol , vol.131 , pp. 283-307
    • Karplus, M.1
  • 28
    • 0001804089 scopus 로고    scopus 로고
    • Aspects of protein reaction dynamics: Deviations from simple behavior
    • Karplus M (2000) Aspects of protein reaction dynamics: Deviations from simple behavior. J Phys Chem B 104:11-27
    • (2000) J Phys Chem B , vol.104 , pp. 11-27
    • Karplus, M.1
  • 29
    • 0014010861 scopus 로고
    • Viscosity and density of aqueous solutions of urea and guanidine hydrochloride
    • Kawahara K, Tanford C (1966) Viscosity and density of aqueous solutions of urea and guanidine hydrochloride. J Biol Chem 241:3228-3232
    • (1966) J Biol Chem , vol.241 , pp. 3228-3232
    • Kawahara, K.1    Tanford, C.2
  • 30
    • 0029323109 scopus 로고
    • A study of cooperative phenyl ring flip motions in glassy polystyrene by molecular simulations
    • Khare R, Paulaitis ME (1995) A study of cooperative phenyl ring flip motions in glassy polystyrene by molecular simulations. Macromolecules 28:4495-4504
    • (1995) Macromolecules , vol.28 , pp. 4495-4504
    • Khare, R.1    Paulaitis, M.E.2
  • 32
    • 14344267020 scopus 로고    scopus 로고
    • Two-state folding of horse ferrocytochrome c: Analyses of linear free energy relationship, chevron curvature, and stopped-flow burst relaxation kinetics
    • Kumar R, Bhuyan AK (2005) Two-state folding of horse ferrocytochrome c: analyses of linear free energy relationship, chevron curvature, and stopped-flow burst relaxation kinetics. Biochemistry 44:3024-3033
    • (2005) Biochemistry , vol.44 , pp. 3024-3033
    • Kumar, R.1    Bhuyan, A.K.2
  • 33
    • 14344262901 scopus 로고    scopus 로고
    • Protein stiffening and entropic stabilization in the subdenaturing limit of guanidine hydrochloride
    • Kumar R, Prabhu NP, Yadaiah M, Bhuyan AK (2004) Protein stiffening and entropic stabilization in the subdenaturing limit of guanidine hydrochloride. Biophys J 87:2656-2662
    • (2004) Biophys J , vol.87 , pp. 2656-2662
    • Kumar, R.1    Prabhu, N.P.2    Yadaiah, M.3    Bhuyan, A.K.4
  • 34
    • 14544269392 scopus 로고    scopus 로고
    • Experimental and computational studies of ring inversion of 1,4-benzodiazepin-2-ones: Implications for memory of chirality transformations
    • Lam PC-H, Carlier PR (2005) Experimental and computational studies of ring inversion of 1,4-benzodiazepin-2-ones: Implications for memory of chirality transformations. J Org Chem 70:1530-1538
    • (2005) J Org Chem , vol.70 , pp. 1530-1538
    • Lam, P.C.-H.1    Carlier, P.R.2
  • 35
    • 0032477750 scopus 로고    scopus 로고
    • Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor
    • Li H, Yamada H, Akasaka K (1998) Effect of pressure on individual hydrogen bonds in proteins. Basic pancreatic trypsin inhibitor. Biochemistry 37:1167-1173
    • (1998) Biochemistry , vol.37 , pp. 1167-1173
    • Li, H.1    Yamada, H.2    Akasaka, K.3
  • 36
    • 33645277619 scopus 로고    scopus 로고
    • Functional role of a protein foldon- an omega-loop foldon controls the alkaline transition in ferricytochrome c
    • Maity H, Rumbley JN, Englander SW (2006) Functional role of a protein foldon- an omega-loop foldon controls the alkaline transition in ferricytochrome c. Proteins 63:349-355
    • (2006) Proteins , vol.63 , pp. 349-355
    • Maity, H.1    Rumbley, J.N.2    Englander, S.W.3
  • 37
    • 0026729426 scopus 로고
    • Protein interactions with urea and guanidinium chloride. A calorimetric study
    • Makhatadze GI, Privalov PL (1992) Protein interactions with urea and guanidinium chloride. A calorimetric study. J Mol Biol 226:491-505
    • (1992) J Mol Biol , vol.226 , pp. 491-505
    • Makhatadze, G.I.1    Privalov, P.L.2
  • 38
    • 0018796418 scopus 로고
    • Picosecond dynamics of tyrosine side chains in proteins
    • McCammon JA, Wolynes PG, Karplus M (1979) Picosecond dynamics of tyrosine side chains in proteins. Biochemistry 18:927-942
    • (1979) Biochemistry , vol.18 , pp. 927-942
    • McCammon, J.A.1    Wolynes, P.G.2    Karplus, M.3
  • 39
    • 0025004276 scopus 로고
    • Rates and energetics of tyrosine ring flips in yeast iso-2-cytochrome c
    • Nall BT, Zuniga EH (1990) Rates and energetics of tyrosine ring flips in yeast iso-2-cytochrome c. Biochemistry 29:7576-7584
    • (1990) Biochemistry , vol.29 , pp. 7576-7584
    • Nall, B.T.1    Zuniga, E.H.2
  • 40
    • 33747065536 scopus 로고    scopus 로고
    • Multiple-basin energy landscapes for large-amplitude conformational motions of proteins: Structure-based molecular dynamics simulations
    • Okazaki K-i, Koga N, Takada S, Onuchic JN et al (2006) Multiple-basin energy landscapes for large-amplitude conformational motions of proteins: Structure-based molecular dynamics simulations. Proc Natl Acad Sci USA 103:11844-11849
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11844-11849
    • Okazaki, K.-I.1    Koga, N.2    Takada, S.3    Onuchic, J.N.4
  • 41
    • 0028981210 scopus 로고
    • Negative activation enthalpies in the kinetics of protein folding
    • Oliveberg M, Tan Y-J, Fersht AR (1995) Negative activation enthalpies in the kinetics of protein folding. Proc Natl Acad Sci USA 92:8926-8929
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8926-8929
    • Oliveberg, M.1    Tan, Y.-J.2    Fersht, A.R.3
  • 42
    • 0027155345 scopus 로고
    • Disulfide bond isomerization in BPTI and BPTI(G36S): An NMR study of correlated mobility in proteins
    • Otting G, Liepinsh E, Wüthrich K (1993) Disulfide bond isomerization in BPTI and BPTI(G36S): An NMR study of correlated mobility in proteins. Biochemistry 32:3571-3582
    • (1993) Biochemistry , vol.32 , pp. 3571-3582
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 43
    • 33751539464 scopus 로고    scopus 로고
    • Protein-protein interactions in the allosteric regulation of protein kinase
    • Pellicena P, Kuriyan J (2006) Protein-protein interactions in the allosteric regulation of protein kinase. Curr Opin Struct Biol 16:702-709
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 702-709
    • Pellicena, P.1    Kuriyan, J.2
  • 44
    • 0028220369 scopus 로고
    • A structural basis for the interaction of urea with lysozyme
    • Pike ACW, Acharya R (1994) A structural basis for the interaction of urea with lysozyme. Protein Sci 3:706-710
    • (1994) Protein Sci , vol.3 , pp. 706-710
    • Pike, A.C.W.1    Acharya, R.2
  • 45
    • 0035868526 scopus 로고    scopus 로고
    • Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics
    • Portman JJ, Takada S, Wolynes PG (2001) Microscopic theory of protein folding rates. II. Local reaction coordinates and chain dynamics. J Chem Phys 114:5082-5096
    • (2001) J Chem Phys , vol.114 , pp. 5082-5096
    • Portman, J.J.1    Takada, S.2    Wolynes, P.G.3
  • 46
    • 0024331090 scopus 로고
    • Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange
    • Roder H (1989) Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. Methods Enzymol 176:446-473
    • (1989) Methods Enzymol , vol.176 , pp. 446-473
    • Roder, H.1
  • 47
    • 0023705432 scopus 로고
    • Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR
    • Roder H, Elöve GA, Englander SW (1988) Structural characterization of folding intermediates in cytochrome c by H-exchange labeling and proton NMR. Nature 335:700-704
    • (1988) Nature , vol.335 , pp. 700-704
    • Roder, H.1    Elöve, G.A.2    Englander, S.W.3
  • 48
    • 0030984109 scopus 로고    scopus 로고
    • Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability
    • Scalley ML, Baker D (1997) Protein folding kinetics exhibit an Arrhenius temperature dependence when corrected for the temperature dependence of protein stability. Proc Natl Acad Sci USA 94:10636-10640
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 10636-10640
    • Scalley, M.L.1    Baker, D.2
  • 49
    • 33846678063 scopus 로고    scopus 로고
    • How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein
    • Shaw BF, Valentine JS (2007) How do ALS-associated mutations in superoxide dismutase 1 promote aggregation of the protein. Trends Biochem Sci 32:78-85
    • (2007) Trends Biochem Sci , vol.32 , pp. 78-85
    • Shaw, B.F.1    Valentine, J.S.2
  • 51
    • 0035941549 scopus 로고    scopus 로고
    • Aromatic ring-flipping in supercooled water: Implications for NMR-based structural biology of proteins
    • Skalicky JJ, Mills JL, Sharma S, Szyperski T (2001) Aromatic ring-flipping in supercooled water: Implications for NMR-based structural biology of proteins. J Am Chem Soc 123:388-397
    • (2001) J Am Chem Soc , vol.123 , pp. 388-397
    • Skalicky, J.J.1    Mills, J.L.2    Sharma, S.3    Szyperski, T.4
  • 52
    • 33744465521 scopus 로고    scopus 로고
    • Modern high resolution NMR for the study of structure, dynamics and interactions of biological macromolecules
    • Stangler T, Hartmann R, Willbold D, Koenig BW (2006) Modern high resolution NMR for the study of structure, dynamics and interactions of biological macromolecules. Z Phys Chem 220:567-613
    • (2006) Z Phys Chem , vol.220 , pp. 567-613
    • Stangler, T.1    Hartmann, R.2    Willbold, D.3    Koenig, B.W.4
  • 53
    • 0025845767 scopus 로고
    • Ligand binding to heme protein: Connection between dynamics and function
    • Steinbach PJ, Ansari A, Berendzen J et al (1991) Ligand binding to heme protein: Connection between dynamics and function. Biochemistry 30:3988-4001
    • (1991) Biochemistry , vol.30 , pp. 3988-4001
    • Steinbach, P.J.1    Ansari, A.2    Berendzen, J.3
  • 54
    • 0035970089 scopus 로고    scopus 로고
    • Convex Arrhenius plots and their interpretation
    • Truhlar DG, Kohen A (2001) Convex Arrhenius plots and their interpretation. Proc Natl Acad Sci USA 98:848-851
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 848-851
    • Truhlar, D.G.1    Kohen, A.2
  • 55
    • 0017314060 scopus 로고
    • Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI)
    • Wagner G, DeMarco A, Wüthrich K (1976) Dynamics of the aromatic amino acid residues in the globular conformation of the basic pancreatic trypsin inhibitor (BPTI). Biohys Struct Mechanism 2:139-158
    • (1976) Biohys Struct Mechanism , vol.2 , pp. 139-158
    • Wagner, G.1    DeMarco, A.2    Wüthrich, K.3
  • 56
    • 0018137537 scopus 로고
    • Dynamic model of globular protein conformations based on NMR studies in solution
    • Wagner G, Wüthrich K (1978) Dynamic model of globular protein conformations based on NMR studies in solution. Nature 275:247-248
    • (1978) Nature , vol.275 , pp. 247-248
    • Wagner, G.1    Wüthrich, K.2
  • 58
    • 0032111921 scopus 로고    scopus 로고
    • NMR detection of slow conformational dynamics in an endonuclease toxin
    • Whittaker SB-M, Boetzel R, MacDonald C, Lian L-Y et al (1998) NMR detection of slow conformational dynamics in an endonuclease toxin. J Biomol NMR 12:145-159
    • (1998) J Biomol NMR , vol.12 , pp. 145-159
    • Whittaker, S.B.-M.1    Boetzel, R.2    MacDonald, C.3    Lian, L.-Y.4
  • 59
    • 0027442944 scopus 로고
    • A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c
    • Wu LC, Laub PB, Elöve GA, Carey J et al (1993) A noncovalent peptide complex as a model for an early folding intermediate of cytochrome c. Biochemistry 32:10271-19276
    • (1993) Biochemistry , vol.32 , pp. 10271-19276
    • Wu, L.C.1    Laub, P.B.2    Elöve, G.A.3    Carey, J.4
  • 60
    • 0016433835 scopus 로고
    • NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor
    • Wüthrich K, Wagner G (1975) NMR investigations of the dynamics of the aromatic amino acid residues in the basic pancreatic trypsin inhibitor. FEBS Lett 50:265-268
    • (1975) FEBS Lett , vol.50 , pp. 265-268
    • Wüthrich, K.1    Wagner, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.