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Volumn 113, Issue 1, 2005, Pages 9-16

Folding rate prediction using n-order contact distance for proteins with two- and three-state folding kinetics

Author keywords

Folding rate; n order contact distance (nOCD); Two and three state folders

Indexed keywords

AMINO ACID SEQUENCE; ARTICLE; CORRELATION COEFFICIENT; KINETICS; NORMAL DISTRIBUTION; PREDICTION; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

EID: 11144269751     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2004.07.036     Document Type: Article
Times cited : (20)

References (62)
  • 1
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • S.E. Jackson How do small single-domain proteins fold? Fold. Des. 3 1998 R81 R91
    • (1998) Fold. Des. , vol.3
    • Jackson, S.E.1
  • 2
    • 0003350984 scopus 로고    scopus 로고
    • Kinetics of protein folding
    • G.L. Hadler W.H. Freeman and Co New York
    • A.R. Fersht Kinetics of protein folding G.L. Hadler Structure and Mechanism in Protein Science 1999 W.H. Freeman and Co New York 540 572
    • (1999) Structure and Mechanism in Protein Science , pp. 540-572
    • Fersht, A.R.1
  • 3
    • 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
    • A.R. Fersht 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 2000 1525 1529
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 1525-1529
    • Fersht, A.R.1
  • 5
    • 0032502839 scopus 로고    scopus 로고
    • Contact order, transition state placement and the refolding rates of single domain proteins
    • K.W. Plaxco, K.T. Simons, and D. Baker Contact order, transition state placement and the refolding rates of single domain proteins J. Mol. Biol. 277 1998 985 994
    • (1998) J. Mol. Biol. , vol.277 , pp. 985-994
    • Plaxco, K.W.1    Simons, K.T.2    Baker, D.3
  • 6
    • 0037402639 scopus 로고    scopus 로고
    • Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics
    • O.V. Galzitskaya, S.O. Garbuzynskiy, D.N. Ivankov, and A.V. Finkelstein Chain length is the main determinant of the folding rate for proteins with three-state folding kinetics Proteins 51 2003 162 166
    • (2003) Proteins , vol.51 , pp. 162-166
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Ivankov, D.N.3    Finkelstein, A.V.4
  • 7
    • 0035967862 scopus 로고    scopus 로고
    • Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: Application of long range order to folding rate prediction
    • M.M. Gromiha, and S. Selvaraj Comparison between long-range interactions and contact order in determining the folding rate of two-state proteins: application of long range order to folding rate prediction J. Mol. Biol. 310 2001 27 32
    • (2001) J. Mol. Biol. , vol.310 , pp. 27-32
    • Gromiha, M.M.1    Selvaraj, S.2
  • 8
    • 0036215854 scopus 로고    scopus 로고
    • Folding rate prediction using total contact distance
    • H.Y. Zhou, and Y.Q. Zhou Folding rate prediction using total contact distance Biophys. J. 82 2002 458 463
    • (2002) Biophys. J. , vol.82 , pp. 458-463
    • Zhou, H.Y.1    Zhou, Y.Q.2
  • 10
    • 0346003776 scopus 로고    scopus 로고
    • Folding rate prediction based on neural network model
    • L.X. Zhang, J. Lin, Z.T. Jiang, and A.G. Xia Folding rate prediction based on neural network model Polymer 44 2003 1751 1757
    • (2003) Polymer , vol.44 , pp. 1751-1757
    • Zhang, L.X.1    Lin, J.2    Jiang, Z.T.3    Xia, A.G.4
  • 11
    • 2942689229 scopus 로고    scopus 로고
    • Prediction of protein folding rates from the amino acid sequence-predicted secondary structure
    • D.N. Ivankov, and A.V. Finkelstein Prediction of protein folding rates from the amino acid sequence-predicted secondary structure Proc. Natl. Acad. Sci. U. S. A. 101 2004 8942 8944
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8942-8944
    • Ivankov, D.N.1    Finkelstein, A.V.2
  • 13
    • 0742304342 scopus 로고    scopus 로고
    • Analysis of structural statistical properties of proteases and nonproteases
    • T.T. Sun, L.X. Zhang, and J. Chen Analysis of structural statistical properties of proteases and nonproteases Polymer 45 2004 1045 1053
    • (2004) Polymer , vol.45 , pp. 1045-1053
    • Sun, T.T.1    Zhang, L.X.2    Chen, J.3
  • 15
    • 0028788480 scopus 로고
    • Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2
    • V. Villegas, A. Azuaga, L. Catasus, D. Reverter, P.L. Mateo, F.X. Aviles, and L. Serrano Evidence for a two-state transition in the folding process of the activation domain of human procarboxypeptidase A2 Biochemistry 34 1995 15105 15110
    • (1995) Biochemistry , vol.34 , pp. 15105-15110
    • Villegas, V.1    Azuaga, A.2    Catasus, L.3    Reverter, D.4    Mateo, P.L.5    Aviles, F.X.6    Serrano, L.7
  • 16
    • 0034671177 scopus 로고    scopus 로고
    • The SH3-fold family: Experimental evidence and prediction of variations in the folding pathways
    • R. Guerois, and L. Serrano The SH3-fold family: experimental evidence and prediction of variations in the folding pathways J. Mol. Biol. 304 2000 967 982
    • (2000) J. Mol. Biol. , vol.304 , pp. 967-982
    • Guerois, R.1    Serrano, L.2
  • 18
    • 0032545150 scopus 로고    scopus 로고
    • Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9
    • B. Kuhlman, D.L. Luisi, P.A. Evans, and D.P. Raleigh Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9 J. Mol. Biol. 284 1998 1661 1670
    • (1998) J. Mol. Biol. , vol.284 , pp. 1661-1670
    • Kuhlman, B.1    Luisi, D.L.2    Evans, P.A.3    Raleigh, D.P.4
  • 19
    • 0032799756 scopus 로고    scopus 로고
    • Folding pathway of FKBP12 and characterisation of the transition state
    • E.R. Main, K.F. Fulton, and S.E. Jackson Folding pathway of FKBP12 and characterisation of the transition state J. Mol. Biol. 291 1999 429 444
    • (1999) J. Mol. Biol. , vol.291 , pp. 429-444
    • Main, E.R.1    Fulton, K.F.2    Jackson, S.E.3
  • 20
    • 0031214363 scopus 로고    scopus 로고
    • A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules
    • K.W. Plaxco, C. Spitzfaden, I.D. Campbell, and C.M. Dobson A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modules J. Mol. Biol. 270 1997 763 770
    • (1997) J. Mol. Biol. , vol.270 , pp. 763-770
    • Plaxco, K.W.1    Spitzfaden, C.2    Campbell, I.D.3    Dobson, C.M.4
  • 21
    • 0034685619 scopus 로고    scopus 로고
    • A breakdown of symmetry in the folding transition state of protein L
    • D.E. Kim, C. Fisher, and D. Baker A breakdown of symmetry in the folding transition state of protein L J. Mol. Biol. 298 2000 971 984
    • (2000) J. Mol. Biol. , vol.298 , pp. 971-984
    • Kim, D.E.1    Fisher, C.2    Baker, D.3
  • 22
    • 0033548553 scopus 로고    scopus 로고
    • Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9
    • N. Ferguson, A.P. Capaldi, R. James, C. Kleanthous, and S.E. Radford Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9 J. Mol. Biol. 286 1999 1597 1608
    • (1999) J. Mol. Biol. , vol.286 , pp. 1597-1608
    • Ferguson, N.1    Capaldi, A.P.2    James, R.3    Kleanthous, C.4    Radford, S.E.5
  • 24
    • 0034737318 scopus 로고    scopus 로고
    • Fast folding of Escherichia coli cyclophilin A: A hypothesis of a unique hydrophobic core with a phenylalanine cluster
    • T. Ikura, T. Hayano, N. Takahashi, and K. Kuwajima Fast folding of Escherichia coli cyclophilin A: a hypothesis of a unique hydrophobic core with a phenylalanine cluster J. Mol. Biol. 297 2000 791 802
    • (2000) J. Mol. Biol. , vol.297 , pp. 791-802
    • Ikura, T.1    Hayano, T.2    Takahashi, N.3    Kuwajima, K.4
  • 25
    • 0031937871 scopus 로고    scopus 로고
    • Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA
    • K.L. Reid, H.M. Rodriguez, B.J. Hillier, and L.M. Gregoret Stability and folding properties of a model beta-sheet protein, Escherichia coli CspA Protein Sci. 7 1998 470 479
    • (1998) Protein Sci. , vol.7 , pp. 470-479
    • Reid, K.L.1    Rodriguez, H.M.2    Hillier, B.J.3    Gregoret, L.M.4
  • 26
    • 0033871567 scopus 로고    scopus 로고
    • Critical role of beta-hairpin formation in protein G folding
    • E.L. McCallister, E. Alm, and D. Baker Critical role of beta-hairpin formation in protein G folding Nat. Struct. Biol. 7 2000 669 673
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 669-673
    • McCallister, E.L.1    Alm, E.2    Baker, D.3
  • 27
    • 0032570543 scopus 로고    scopus 로고
    • Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy
    • J.I. Guijarro, C.J. Morton, K.W. Plaxco, I.D. Campbell, and C.M. Dobson Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopy J. Mol. Biol. 276 1998 657 667
    • (1998) J. Mol. Biol. , vol.276 , pp. 657-667
    • Guijarro, J.I.1    Morton, C.J.2    Plaxco, K.W.3    Campbell, I.D.4    Dobson, C.M.5
  • 30
    • 0032718386 scopus 로고    scopus 로고
    • Salt-induced detour through compact regions of the protein folding landscape
    • D.E. Otzen, and M. Oliveberg Salt-induced detour through compact regions of the protein folding landscape Proc. Natl. Acad. Sci. U. S. A. 96 1999 11746 11751
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11746-11751
    • Otzen, D.E.1    Oliveberg, M.2
  • 32
    • 0029760326 scopus 로고    scopus 로고
    • Different folding transition states may result in the same native structure
    • A.R. Viguera, L. Serrano, and M. Wilmanns Different folding transition states may result in the same native structure Nat. Struct. Biol. 3 1996 874 880
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 874-880
    • Viguera, A.R.1    Serrano, L.2    Wilmanns, M.3
  • 33
    • 0031444104 scopus 로고    scopus 로고
    • Folding dynamics of the src SH3 domain
    • V.P. Grantcharova, and D. Baker Folding dynamics of the src SH3 domain Biochemistry 36 1997 15685 15692
    • (1997) Biochemistry , vol.36 , pp. 15685-15692
    • Grantcharova, V.P.1    Baker, D.2
  • 34
    • 0031214818 scopus 로고    scopus 로고
    • Folding and stability of afibronectin type III domain of human tenascin
    • J. Clarke, S.J. Hamill, and C.M. Johnson Folding and stability of afibronectin type III domain of human tenascin J. Mol. Biol. 270 1997 771 778
    • (1997) J. Mol. Biol. , vol.270 , pp. 771-778
    • Clarke, J.1    Hamill, S.J.2    Johnson, C.M.3
  • 35
    • 0030750236 scopus 로고    scopus 로고
    • High-energy channeling in protein folding
    • M. Silow, and M. Oliverberg High-energy channeling in protein folding Biochemistry 36 1997 7633 7637
    • (1997) Biochemistry , vol.36 , pp. 7633-7637
    • Silow, M.1    Oliverberg, M.2
  • 36
    • 0033200251 scopus 로고    scopus 로고
    • Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway
    • J. Clarke, E. Cota, S.B. Fowler, and S.J. Hamill Folding studies of immunoglobulin-like beta-sandwich proteins suggest that they share a common folding pathway Struct. Fold. Des. 7 1999 1145 1153
    • (1999) Struct. Fold. Des. , vol.7 , pp. 1145-1153
    • Clarke, J.1    Cota, E.2    Fowler, S.B.3    Hamill, S.J.4
  • 37
    • 0033535839 scopus 로고    scopus 로고
    • Cytochrome b562 folding triggered by electron transfer: Approaching the speed limit for formation of a four-helix-bundle protein
    • P. Wittung-Stafshede, J.C. Lee, J.R. Winkler, and H.B. Gray Cytochrome b562 folding triggered by electron transfer: approaching the speed limit for formation of a four-helix-bundle protein Proc. Natl. Acad. Sci. U. S. A. 96 1999 6587 6590
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 6587-6590
    • Wittung-Stafshede, P.1    Lee, J.C.2    Winkler, J.R.3    Gray, H.B.4
  • 39
    • 0026345750 scopus 로고
    • Folding of chymotrypsin inhibitor 2: 1. Evidence for a two-state transition
    • S.E. Jackson, and A.R. Fersht Folding of chymotrypsin inhibitor 2: 1. Evidence for a two-state transition Biochemistry 30 1991 10428 10435
    • (1991) Biochemistry , vol.30 , pp. 10428-10435
    • Jackson, S.E.1    Fersht, A.R.2
  • 40
    • 0033527587 scopus 로고    scopus 로고
    • Submillisecond folding of the peripheral subunit-binding domain
    • S. Spector, and D.P. Raleigh Submillisecond folding of the peripheral subunit-binding domain J. Mol. Biol. 293 1999 763 768
    • (1999) J. Mol. Biol. , vol.293 , pp. 763-768
    • Spector, S.1    Raleigh, D.P.2
  • 41
    • 0032514727 scopus 로고    scopus 로고
    • Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores
    • S.E. Choe, P.T. Matsudaira, J. Osterhout, G. Wagner, and E.I. Shakhnovich Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores Biochemistry 37 1998 14508 14518
    • (1998) Biochemistry , vol.37 , pp. 14508-14518
    • Choe, S.E.1    Matsudaira, P.T.2    Osterhout, J.3    Wagner, G.4    Shakhnovich, E.I.5
  • 42
    • 0033534586 scopus 로고    scopus 로고
    • Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin
    • S. Cavagnero, H.J. Dyson, and P.E. Wright Effect of H helix destabilizing mutations on the kinetic and equilibrium folding of apomyoglobin J. Mol. Biol. 285 1999 269 282
    • (1999) J. Mol. Biol. , vol.285 , pp. 269-282
    • Cavagnero, S.1    Dyson, H.J.2    Wright, P.E.3
  • 43
    • 0032548994 scopus 로고    scopus 로고
    • Thermodynamic stability and folding of GroEL minichaperones
    • R. Golbik, R. Zahn, S.E. Harding, and A.R. Fersht Thermodynamic stability and folding of GroEL minichaperones J. Mol. Biol. 276 1998 505 515
    • (1998) J. Mol. Biol. , vol.276 , pp. 505-515
    • Golbik, R.1    Zahn, R.2    Harding, S.E.3    Fersht, A.R.4
  • 44
  • 45
    • 0027385015 scopus 로고
    • The refolding of cis- and transpeptidylprolyl isomers of barstar
    • G. Schreiber, and A.R. Fersht The refolding of cis- and transpeptidylprolyl isomers of barstar Biochemistry 32 1993 11195 11203
    • (1993) Biochemistry , vol.32 , pp. 11195-11203
    • Schreiber, G.1    Fersht, A.R.2
  • 46
    • 0032190351 scopus 로고    scopus 로고
    • Folding mechanism of three structurally similar beta-sheet proteins
    • L.L. Burns, P.M. Dalessio, and I.J. Ropson Folding mechanism of three structurally similar beta-sheet proteins Proteins 33 1998 107 118
    • (1998) Proteins , vol.33 , pp. 107-118
    • Burns, L.L.1    Dalessio, P.M.2    Ropson, I.J.3
  • 47
    • 0034620582 scopus 로고    scopus 로고
    • Beta-sheet proteins with nearly identical structures have different folding intermediates
    • P.M. Dalessio, and I.J. Ropson Beta-sheet proteins with nearly identical structures have different folding intermediates Biochemistry 39 2000 860 871
    • (2000) Biochemistry , vol.39 , pp. 860-871
    • Dalessio, P.M.1    Ropson, I.J.2
  • 48
    • 0033957144 scopus 로고    scopus 로고
    • Folding of beta-sandwich proteins: Three-state transition of a fibronectin type III module
    • E. Cota, and J. Clarke Folding of beta-sandwich proteins: three-state transition of a fibronectin type III module Protein Sci. 9 2000 112 120
    • (2000) Protein Sci. , vol.9 , pp. 112-120
    • Cota, E.1    Clarke, J.2
  • 49
    • 0030871209 scopus 로고    scopus 로고
    • Acquisition of native beta-strand topology during the rapid collapse phase of protein folding
    • M.J. Parker, C.E. Dempsey, M. Lorch, and A.R. Clarke Acquisition of native beta-strand topology during the rapid collapse phase of protein folding Biochemistry 36 1997 13396 13405
    • (1997) Biochemistry , vol.36 , pp. 13396-13405
    • Parker, M.J.1    Dempsey, C.E.2    Lorch, M.3    Clarke, A.R.4
  • 50
    • 0032190351 scopus 로고    scopus 로고
    • Folding mechanism of three structurally similar beta-sheet proteins
    • L.L. Burns, P.M. Dalessio, and I.J. Ropson Folding mechanism of three structurally similar beta-sheet proteins Proteins 33 1998 107 118
    • (1998) Proteins , vol.33 , pp. 107-118
    • Burns, L.L.1    Dalessio, P.M.2    Ropson, I.J.3
  • 51
    • 0028791393 scopus 로고
    • An integrated kinetic analysis of intermediates and transition states in protein folding reactions
    • M.J. Parker, J. Spencer, and A.R. Clarke An integrated kinetic analysis of intermediates and transition states in protein folding reactions J. Mol. Biol. 253 1995 771 786
    • (1995) J. Mol. Biol. , vol.253 , pp. 771-786
    • Parker, M.J.1    Spencer, J.2    Clarke, A.R.3
  • 52
    • 0030347884 scopus 로고    scopus 로고
    • The development of tertiary interactions during the folding of a large protein
    • M.J. Parker, R.B. Sessions, I.G. Badcoe, and A.R. Clarke The development of tertiary interactions during the folding of a large protein Fold. Des. 1 1996 145 156
    • (1996) Fold. Des. , vol.1 , pp. 145-156
    • Parker, M.J.1    Sessions, R.B.2    Badcoe, I.G.3    Clarke, A.R.4
  • 53
    • 0028258789 scopus 로고
    • Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements
    • K. Ogasahara, and K. Yutani Unfolding-refolding kinetics of the tryptophan synthase alpha subunit by CD and fluorescence measurements J. Mol. Biol. 236 1994 1227 1240
    • (1994) J. Mol. Biol. , vol.236 , pp. 1227-1240
    • Ogasahara, K.1    Yutani, K.2
  • 54
    • 0025216077 scopus 로고
    • An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a "molten globule"
    • M.E. Goldberg, G.V. Semisotnov, B. Friguet, K. Kuwajima, O.B. Ptitsyn, and S. Sugai An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a "molten globule" FEBS Lett. 263 1990 51 56
    • (1990) FEBS Lett. , vol.263 , pp. 51-56
    • Goldberg, M.E.1    Semisotnov, G.V.2    Friguet, B.3    Kuwajima, K.4    Ptitsyn, O.B.5    Sugai, S.6
  • 55
    • 0027315969 scopus 로고
    • A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: Verification and refinement of a four-channel model
    • P.A. Jennings, B.E. Finn, B.E. Jones, and C.R. Matthews A reexamination of the folding mechanism of dihydrofolate reductase from Escherichia coli: verification and refinement of a four-channel model Biochemistry 32 1993 3783 3789
    • (1993) Biochemistry , vol.32 , pp. 3783-3789
    • Jennings, P.A.1    Finn, B.E.2    Jones, B.E.3    Matthews, C.R.4
  • 56
    • 0034650515 scopus 로고    scopus 로고
    • The folding pathway of the cell-cycle regulatory protein p13suc1: Clues for the mechanism of domain swapping
    • J.W. Schymkowitz, F. Rousseau, L.R. Irvine, and L.S. Itzhaki The folding pathway of the cell-cycle regulatory protein p13suc1: clues for the mechanism of domain swapping Struct. Fold. Des. 8 2000 89 100
    • (2000) Struct. Fold. Des. , vol.8 , pp. 89-100
    • Schymkowitz, J.W.1    Rousseau, F.2    Irvine, L.R.3    Itzhaki, L.S.4
  • 57
    • 0034984382 scopus 로고    scopus 로고
    • Mapping the folding pathway of an immunoglobulin domain. Structural detail from phi value analysis and movement of the transition state
    • S.B. Fowler, and J. Clarke Mapping the folding pathway of an immunoglobulin domain. Structural detail from phi value analysis and movement of the transition state Structure 9 2001 355 366
    • (2001) Structure , vol.9 , pp. 355-366
    • Fowler, S.B.1    Clarke, J.2
  • 58
    • 0030057477 scopus 로고    scopus 로고
    • Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
    • S. Khorasanizadeh, I.D. Peters, and H. Roder Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues Nat. Struct. Biol. 3 1996 193 205
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 193-205
    • Khorasanizadeh, S.1    Peters, I.D.2    Roder, H.3
  • 61
    • 0033550298 scopus 로고    scopus 로고
    • The cooperativity of burst phase reactions explored
    • M.J. Parker, and S. Marqusee The cooperativity of burst phase reactions explored J. Mol. Biol. 293 1999 1195 1210
    • (1999) J. Mol. Biol. , vol.293 , pp. 1195-1210
    • Parker, M.J.1    Marqusee, S.2
  • 62
    • 0028176281 scopus 로고
    • Kinetic characterization of the chemotactic protein from Escherichia coli, Che Y. Kinetic analysis of the inverse hydrophobic effect
    • V. Munoz, E.M. Lopez, M. Jager, and L. Serrano Kinetic characterization of the chemotactic protein from Escherichia coli, Che Y. Kinetic analysis of the inverse hydrophobic effect Biochemistry 33 1994 5858 5866
    • (1994) Biochemistry , vol.33 , pp. 5858-5866
    • Munoz, V.1    Lopez, E.M.2    Jager, M.3    Serrano, L.4


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