메뉴 건너뛰기




Volumn 53, Issue 19, 2014, Pages 3169-3178

Fast closure of n-terminal long loops but slow formation of β strands precedes the folding transition state of escherichia coli adenylate kinase

Author keywords

[No Author keywords available]

Indexed keywords

ENERGY TRANSFER; ENZYMES;

EID: 84900993074     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500069w     Document Type: Article
Times cited : (11)

References (56)
  • 1
    • 0033080081 scopus 로고    scopus 로고
    • Is protein folding hierarchic? II. Folding intermediates and transition states
    • Baldwin, R. L. and Rose, G. D. (1999) Is protein folding hierarchic? II. Folding intermediates and transition states Trends Biochem. Sci. 24, 77-83
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 77-83
    • Baldwin, R.L.1    Rose, G.D.2
  • 2
    • 42449151176 scopus 로고    scopus 로고
    • Protein folding and misfolding: Mechanism and principles
    • Englander, S. W., Mayne, L., and Krishna, M. M. (2007) Protein folding and misfolding: Mechanism and principles Q. Rev. Biophys. 40, 287-326
    • (2007) Q. Rev. Biophys. , vol.40 , pp. 287-326
    • Englander, S.W.1    Mayne, L.2    Krishna, M.M.3
  • 3
    • 33745955427 scopus 로고    scopus 로고
    • Specificity of the initial collapse in the folding of the cold shock protein
    • Magg, C., Kubelka, J., Holtermann, G., Haas, E., and Schmid, F. X. (2006) Specificity of the initial collapse in the folding of the cold shock protein J. Mol. Biol. 360, 1067-1080
    • (2006) J. Mol. Biol. , vol.360 , pp. 1067-1080
    • Magg, C.1    Kubelka, J.2    Holtermann, G.3    Haas, E.4    Schmid, F.X.5
  • 4
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht, A. R. (1997) Nucleation mechanisms in protein folding Curr. Opin. Struct. Biol. 7, 3-9
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 3-9
    • Fersht, A.R.1
  • 5
    • 0025906282 scopus 로고
    • Polymer principles in protein structure and stability
    • Chan, H. S. and Dill, K. A. (1991) Polymer principles in protein structure and stability Annu. Rev. Biophys. Biophys. Chem. 20, 447-490
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 447-490
    • Chan, H.S.1    Dill, K.A.2
  • 6
    • 79958057466 scopus 로고    scopus 로고
    • Minireview: Structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering
    • Kathuria, S. V., Guo, L., Graceffa, R., Barrea, R., Nobrega, R. P., Matthews, C. R., Irving, T. C., and Bilsel, O. (2011) Minireview: Structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scattering Biopolymers 95, 550-558
    • (2011) Biopolymers , vol.95 , pp. 550-558
    • Kathuria, S.V.1    Guo, L.2    Graceffa, R.3    Barrea, R.4    Nobrega, R.P.5    Matthews, C.R.6    Irving, T.C.7    Bilsel, O.8
  • 7
    • 33744937937 scopus 로고    scopus 로고
    • Early events in protein folding explored by rapid mixing methods
    • Roder, H., Maki, K., and Cheng, H. (2006) Early events in protein folding explored by rapid mixing methods Chem. Rev. 106, 1836-1861
    • (2006) Chem. Rev. , vol.106 , pp. 1836-1861
    • Roder, H.1    Maki, K.2    Cheng, H.3
  • 9
    • 0035252350 scopus 로고    scopus 로고
    • Three key residues form a critical contact network in a protein folding transition state
    • Vendruscolo, M., Paci, E., Dobson, C. M., and Karplus, M. (2001) Three key residues form a critical contact network in a protein folding transition state Nature 409, 641-645
    • (2001) Nature , vol.409 , pp. 641-645
    • Vendruscolo, M.1    Paci, E.2    Dobson, C.M.3    Karplus, M.4
  • 10
    • 0034652206 scopus 로고    scopus 로고
    • Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism
    • Fersht, A. R. (2000) Transition-state structure as a unifying basis in protein-folding mechanisms: Contact order, chain topology, stability, and the extended nucleus mechanism Proc. Natl. Acad. Sci. U.S.A. 97, 1525-1529
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 11
    • 2342451295 scopus 로고    scopus 로고
    • Transition states for protein folding have native topologies despite high structural variability
    • Lindorff-Larsen, K., Vendruscolo, M., Paci, E., and Dobson, C. M. (2004) Transition states for protein folding have native topologies despite high structural variability Nat. Struct. Mol. Biol. 11, 443-449
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 443-449
    • Lindorff-Larsen, K.1    Vendruscolo, M.2    Paci, E.3    Dobson, C.M.4
  • 12
    • 0020024242 scopus 로고
    • Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding
    • Kim, P. S. and Baldwin, R. L. (1982) Specific intermediates in the folding reactions of small proteins and the mechanism of protein folding Annu. Rev. Biochem. 51, 459-489
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 459-489
    • Kim, P.S.1    Baldwin, R.L.2
  • 14
    • 0000355428 scopus 로고
    • Respective roles of short- and long-range interactions in protein folding
    • Go, N. and Taketomi, H. (1978) Respective roles of short- and long-range interactions in protein folding Proc. Natl. Acad. Sci. U.S.A. 75, 559-563
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 559-563
    • Go, N.1    Taketomi, H.2
  • 15
    • 0016696599 scopus 로고
    • Studies on protein folding, unfolding and fluctuations by computer simulation. I the effect of specific amino acid sequence represented by specific inter-unit interactions
    • Taketomi, H., Ueda, Y., and Go, N. (1975) Studies on protein folding, unfolding and fluctuations by computer simulation. I. The effect of specific amino acid sequence represented by specific inter-unit interactions Int. J. Pept. Protein Res. 7, 445-459
    • (1975) Int. J. Pept. Protein Res. , vol.7 , pp. 445-459
    • Taketomi, H.1    Ueda, Y.2    Go, N.3
  • 17
    • 0029115970 scopus 로고
    • Optimal local propensities for model proteins
    • Govindarajan, S. and Goldstein, R. A. (1995) Optimal local propensities for model proteins Proteins 22, 413-418
    • (1995) Proteins , vol.22 , pp. 413-418
    • Govindarajan, S.1    Goldstein, R.A.2
  • 18
    • 0029155772 scopus 로고
    • Impact of local and non-local interactions on thermodynamics and kinetics of protein folding
    • Abkevich, V. I., Gutin, A. M., and Shakhnovich, E. I. (1995) Impact of local and non-local interactions on thermodynamics and kinetics of protein folding J. Mol. Biol. 252, 460-471
    • (1995) J. Mol. Biol. , vol.252 , pp. 460-471
    • Abkevich, V.I.1    Gutin, A.M.2    Shakhnovich, E.I.3
  • 19
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • Anfinsen, C. B. and Scheraga, H. A. (1975) Experimental and theoretical aspects of protein folding Adv. Protein Chem. 29, 205-300
    • (1975) Adv. Protein Chem. , vol.29 , pp. 205-300
    • Anfinsen, C.B.1    Scheraga, H.A.2
  • 20
    • 0001756859 scopus 로고
    • Is there a single pathway for the folding of a polypeptide chain?
    • Harrison, S. C. and Durbin, R. (1985) Is there a single pathway for the folding of a polypeptide chain? Proc. Natl. Acad. Sci. U.S.A. 82, 4028-4030
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 4028-4030
    • Harrison, S.C.1    Durbin, R.2
  • 21
    • 0026447086 scopus 로고
    • Extracting information on folding from the amino acid sequence: Accurate predictions for protein regions with preferred conformation in the absence of tertiary interactions
    • Rooman, M. J., Kocher, J. P., and Wodak, S. J. (1992) Extracting information on folding from the amino acid sequence: Accurate predictions for protein regions with preferred conformation in the absence of tertiary interactions Biochemistry 31, 10226-10238
    • (1992) Biochemistry , vol.31 , pp. 10226-10238
    • Rooman, M.J.1    Kocher, J.P.2    Wodak, S.J.3
  • 22
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
    • Wright, P. E., Dyson, H. J., and Lerner, R. A. (1988) Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding Biochemistry 27, 7167-7175
    • (1988) Biochemistry , vol.27 , pp. 7167-7175
    • Wright, P.E.1    Dyson, H.J.2    Lerner, R.A.3
  • 24
    • 0038630483 scopus 로고    scopus 로고
    • Folding rates and low-entropy-loss routes of two-state proteins
    • Weikl, T. R. and Dill, K. A. (2003) Folding rates and low-entropy-loss routes of two-state proteins J. Mol. Biol. 329, 585-598
    • (2003) J. Mol. Biol. , vol.329 , pp. 585-598
    • Weikl, T.R.1    Dill, K.A.2
  • 25
    • 0015933325 scopus 로고
    • Evidence for nucleation in the folding of reduced hen egg lysozyme
    • Ristow, S. S. and Wetlaufer, D. B. (1973) Evidence for nucleation in the folding of reduced hen egg lysozyme Biochem. Biophys. Res. Commun. 50, 544-550
    • (1973) Biochem. Biophys. Res. Commun. , vol.50 , pp. 544-550
    • Ristow, S.S.1    Wetlaufer, D.B.2
  • 26
    • 23644456329 scopus 로고    scopus 로고
    • The effect of long-range interactions on the secondary structure formation of proteins
    • Kihara, D. (2005) The effect of long-range interactions on the secondary structure formation of proteins Protein Sci. 14, 1955-1963
    • (2005) Protein Sci. , vol.14 , pp. 1955-1963
    • Kihara, D.1
  • 27
    • 0028936789 scopus 로고
    • Nonlocal Interactions Stabilize Long-Range Loops in the Initial Folding Intermediates of Reduced Bovine Pancreatic Trypsin-Inhibitor
    • Ittah, V. and Haas, E. (1995) Nonlocal Interactions Stabilize Long-Range Loops in the Initial Folding Intermediates of Reduced Bovine Pancreatic Trypsin-Inhibitor Biochemistry 34, 4493-4506
    • (1995) Biochemistry , vol.34 , pp. 4493-4506
    • Ittah, V.1    Haas, E.2
  • 28
    • 18744389451 scopus 로고    scopus 로고
    • The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements
    • Haas, E. (2005) The study of protein folding and dynamics by determination of intramolecular distance distributions and their fluctuations using ensemble and single-molecule FRET measurements ChemPhysChem 6, 858-870
    • (2005) ChemPhysChem , vol.6 , pp. 858-870
    • Haas, E.1
  • 29
    • 0022981913 scopus 로고
    • Loops in globular proteins: A novel category of secondary structure
    • Leszczynski, J. F. and Rose, G. D. (1986) Loops in globular proteins: A novel category of secondary structure Science 234, 849-855
    • (1986) Science , vol.234 , pp. 849-855
    • Leszczynski, J.F.1    Rose, G.D.2
  • 30
    • 84877022104 scopus 로고    scopus 로고
    • The loop hypothesis: Contribution of early formed specific non-local interactions to the determination of protein folding pathways
    • Orevi, T., Rahamim, G., Hazan, G., Amir, D., and Haas, E. (2013) The loop hypothesis: Contribution of early formed specific non-local interactions to the determination of protein folding pathways Biophys. Rev. 5, 85-98
    • (2013) Biophys. Rev. , vol.5 , pp. 85-98
    • Orevi, T.1    Rahamim, G.2    Hazan, G.3    Amir, D.4    Haas, E.5
  • 31
    • 0025993941 scopus 로고
    • Conformational studies of a peptide corresponding to a region of the C-terminus of ribonuclease A: Implications as a potential chain-folding initiation site
    • Beals, J. M., Haas, E., Krausz, S., and Scheraga, H. A. (1991) Conformational studies of a peptide corresponding to a region of the C-terminus of ribonuclease A: Implications as a potential chain-folding initiation site Biochemistry 30, 7680-7692
    • (1991) Biochemistry , vol.30 , pp. 7680-7692
    • Beals, J.M.1    Haas, E.2    Krausz, S.3    Scheraga, H.A.4
  • 32
    • 0028884985 scopus 로고
    • Sequential domain unfolding in phosphoglycerate kinase: Fluorescence intensity and anisotropy stopped-flow kinetics of several tryptophan mutants
    • Beechem, J. M., Sherman, M. A., and Mas, M. T. (1995) Sequential domain unfolding in phosphoglycerate kinase: Fluorescence intensity and anisotropy stopped-flow kinetics of several tryptophan mutants Biochemistry 34, 13943-13948
    • (1995) Biochemistry , vol.34 , pp. 13943-13948
    • Beechem, J.M.1    Sherman, M.A.2    Mas, M.T.3
  • 33
    • 0000192202 scopus 로고    scopus 로고
    • An instrument for time resolved monitoring of fast chemical transitions: Application to the kinetics of refolding of a globular protein
    • Ratner, V. and Haas, E. (1998) An instrument for time resolved monitoring of fast chemical transitions: Application to the kinetics of refolding of a globular protein Rev. Sci. Instrum. 69, 2147-2154
    • (1998) Rev. Sci. Instrum. , vol.69 , pp. 2147-2154
    • Ratner, V.1    Haas, E.2
  • 34
    • 84865756639 scopus 로고    scopus 로고
    • An instrument for fast acquisition of fluorescence decay curves at picosecond resolution designed for "double kinetics" experiments: Application to FRET study of protein folding
    • Ben Ishay, E., Hazan, G., Rahamim, G., Amir, D., and Haas, E. (2012) An instrument for fast acquisition of fluorescence decay curves at picosecond resolution designed for "double kinetics" experiments: Application to FRET study of protein folding Rev. Sci. Instrum. 83, 084301
    • (2012) Rev. Sci. Instrum. , vol.83 , pp. 084301
    • Ben Ishay, E.1    Hazan, G.2    Rahamim, G.3    Amir, D.4    Haas, E.5
  • 35
    • 24044490917 scopus 로고    scopus 로고
    • Fast collapse but slow formation of secondary structure elements in the refolding transition of E coli adenylate kinase
    • Ratner, V., Amir, D., Kahana, E., and Haas, E. (2005) Fast collapse but slow formation of secondary structure elements in the refolding transition of E coli adenylate kinase J. Mol. Biol. 352, 683-699
    • (2005) J. Mol. Biol. , vol.352 , pp. 683-699
    • Ratner, V.1    Amir, D.2    Kahana, E.3    Haas, E.4
  • 36
    • 0034705335 scopus 로고    scopus 로고
    • Determination of intramolecular distance distribution during protein folding on the millisecond timescale
    • Ratner, V., Sinev, M., and Haas, E. (2000) Determination of intramolecular distance distribution during protein folding on the millisecond timescale J. Mol. Biol. 299, 1363-1371
    • (2000) J. Mol. Biol. , vol.299 , pp. 1363-1371
    • Ratner, V.1    Sinev, M.2    Haas, E.3
  • 37
    • 84867258888 scopus 로고    scopus 로고
    • Fast subdomain folding prior to the global refolding transition of E coli adenylate kinase: A double kinetics study
    • Ben Ishay, E., Rahamim, G., Orevi, T., Hazan, G., Amir, D., and Haas, E. (2012) Fast subdomain folding prior to the global refolding transition of E coli adenylate kinase: A double kinetics study J. Mol. Biol. 423, 613-623
    • (2012) J. Mol. Biol. , vol.423 , pp. 613-623
    • Ben Ishay, E.1    Rahamim, G.2    Orevi, T.3    Hazan, G.4    Amir, D.5    Haas, E.6
  • 38
    • 58149396567 scopus 로고    scopus 로고
    • Early closure of a long loop in the refolding of adenylate kinase: A possible key role of non-local interactions in the initial folding steps
    • Orevi, T., Ben Ishay, E., Pirchi, M., Jacob, M. H., Amir, D., and Haas, E. (2009) Early closure of a long loop in the refolding of adenylate kinase: A possible key role of non-local interactions in the initial folding steps J. Mol. Biol. 385, 1230-1242
    • (2009) J. Mol. Biol. , vol.385 , pp. 1230-1242
    • Orevi, T.1    Ben Ishay, E.2    Pirchi, M.3    Jacob, M.H.4    Amir, D.5    Haas, E.6
  • 39
    • 0034117516 scopus 로고    scopus 로고
    • Design consideration and probes for fluorescence resonance energy transfer studies
    • Sinev, M., Landsmann, P., Sineva, E., Ittah, V., and Haas, E. (2000) Design consideration and probes for fluorescence resonance energy transfer studies Bioconjugate Chem. 11, 352-362
    • (2000) Bioconjugate Chem. , vol.11 , pp. 352-362
    • Sinev, M.1    Landsmann, P.2    Sineva, E.3    Ittah, V.4    Haas, E.5
  • 40
    • 0014429881 scopus 로고
    • Initial velocity and equilibrium kinetics of myokinase
    • Rhoads, D. G. and Lowenstein, J. M. (1968) Initial velocity and equilibrium kinetics of myokinase J. Biol. Chem. 243, 3963-3972
    • (1968) J. Biol. Chem. , vol.243 , pp. 3963-3972
    • Rhoads, D.G.1    Lowenstein, J.M.2
  • 41
    • 0036737063 scopus 로고    scopus 로고
    • A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies
    • Ratner, V., Kahana, E., Eichler, M., and Haas, E. (2002) A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies Bioconjugate Chem. 13, 1163-1170
    • (2002) Bioconjugate Chem. , vol.13 , pp. 1163-1170
    • Ratner, V.1    Kahana, E.2    Eichler, M.3    Haas, E.4
  • 42
    • 27144464106 scopus 로고    scopus 로고
    • Predicting reactivities of protein surface cysteines as part of a strategy for selective multiple labeling
    • Jacob, M. H., Amir, D., Ratner, V., Gussakowsky, E., and Haas, E. (2005) Predicting reactivities of protein surface cysteines as part of a strategy for selective multiple labeling Biochemistry 44, 13664-13672
    • (2005) Biochemistry , vol.44 , pp. 13664-13672
    • Jacob, M.H.1    Amir, D.2    Ratner, V.3    Gussakowsky, E.4    Haas, E.5
  • 43
    • 78751591016 scopus 로고    scopus 로고
    • Segmental Conformational Disorder and Dynamics in the Intrinsically Disordered Protein α-Synuclein and Its Chain Length Dependence
    • Grupi, A. and Haas, E. (2011) Segmental Conformational Disorder and Dynamics in the Intrinsically Disordered Protein α-Synuclein and Its Chain Length Dependence J. Mol. Biol. 405, 1267-1283
    • (2011) J. Mol. Biol. , vol.405 , pp. 1267-1283
    • Grupi, A.1    Haas, E.2
  • 45
    • 0024553479 scopus 로고
    • Folding and dynamics of globular proteins studied by time resolved fluorescence spectroscopy
    • Haas, E. (1989) Folding and dynamics of globular proteins studied by time resolved fluorescence spectroscopy Prog. Clin. Biol. Res. 289, 157-170
    • (1989) Prog. Clin. Biol. Res. , vol.289 , pp. 157-170
    • Haas, E.1
  • 47
    • 0026653655 scopus 로고
    • Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR
    • Englander, S. W. and 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
  • 48
    • 51649106422 scopus 로고    scopus 로고
    • Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein
    • Wu, Y., Kondrashkina, E., Kayatekin, C., Matthews, C. R., and Bilsel, O. (2008) Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein Proc. Natl. Acad. Sci. U.S.A. 105, 13367-13372
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 13367-13372
    • Wu, Y.1    Kondrashkina, E.2    Kayatekin, C.3    Matthews, C.R.4    Bilsel, O.5
  • 49
    • 84859266139 scopus 로고    scopus 로고
    • Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state
    • Yoo, T. Y., Meisburger, S. P., Hinshaw, J., Pollack, L., Haran, G., Sosnick, T. R., and Plaxco, K. (2012) Small-angle X-ray scattering and single-molecule FRET spectroscopy produce highly divergent views of the low-denaturant unfolded state J. Mol. Biol. 418, 226-236
    • (2012) J. Mol. Biol. , vol.418 , pp. 226-236
    • Yoo, T.Y.1    Meisburger, S.P.2    Hinshaw, J.3    Pollack, L.4    Haran, G.5    Sosnick, T.R.6    Plaxco, K.7
  • 50
    • 84857033993 scopus 로고    scopus 로고
    • How, when and why proteins collapse: The relation to folding
    • Haran, G. (2012) How, when and why proteins collapse: The relation to folding Curr. Opin. Struct. Biol. 22, 14-20
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 14-20
    • Haran, G.1
  • 51
    • 58149396567 scopus 로고    scopus 로고
    • Early closure of a long loop in the refolding of adenylate kinase: A possible key role of non-local interactions in the initial folding steps
    • Orevi, T., Ben Ishay, E., Pirchi, M., Jacob, M. H., Amir, D., and Haas, E. (2009) Early closure of a long loop in the refolding of adenylate kinase: A possible key role of non-local interactions in the initial folding steps J. Mol. Biol. 385, 1230-1242
    • (2009) J. Mol. Biol. , vol.385 , pp. 1230-1242
    • Orevi, T.1    Ben Ishay, E.2    Pirchi, M.3    Jacob, M.H.4    Amir, D.5    Haas, E.6
  • 53
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • Plaxco, K. W., Simons, K. T., and Baker, D. (1998) Contact order, transition state placement and the refolding rates of single domain proteins J. Mol. Biol. 277, 985-994
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 54
    • 0000248317 scopus 로고    scopus 로고
    • Sequential Collapse Model for Protein Folding Pathways
    • Bergasa-Caceres, F., Ronneberg, T. A., and Rabitz, H. (1999) Sequential Collapse Model for Protein Folding Pathways J. Phys. Chem. B 103, 9749-9758
    • (1999) J. Phys. Chem. B , vol.103 , pp. 9749-9758
    • Bergasa-Caceres, F.1    Ronneberg, T.A.2    Rabitz, H.3
  • 55
    • 0037221599 scopus 로고    scopus 로고
    • Is there a unifying mechanism for protein folding?
    • Daggett, V. and Fersht, A. R. (2003) Is there a unifying mechanism for protein folding? Trends Biochem. Sci. 28, 18-25
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 18-25
    • Daggett, V.1    Fersht, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.