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Volumn 406, Issue 3, 2011, Pages 430-442

Spontaneous proton transfer to a conserved intein residue determines on-pathway protein splicing

Author keywords

FRET assay; intein mutagenesis; protein splicing; quantum mechanics; reaction mechanism

Indexed keywords

ASPARTIC ACID; EXTEIN; INTEIN;

EID: 79551681995     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.12.024     Document Type: Article
Times cited : (22)

References (62)
  • 1
    • 0028214350 scopus 로고
    • Protein splicing elements: Inteins and exteins-a definition of terms and recommended nomenclature
    • Perler F.B., Davis E.O., Dean G.E., Gimble F.S., Jack W.E., and Neff N. Protein splicing elements: inteins and exteins-a definition of terms and recommended nomenclature Nucleic Acids Res. 22 1994 1125 1127
    • (1994) Nucleic Acids Res. , vol.22 , pp. 1125-1127
    • Perler, F.B.1    Davis, E.O.2    Dean, G.E.3    Gimble, F.S.4    Jack, W.E.5    Neff, N.6
  • 5
    • 11844291287 scopus 로고    scopus 로고
    • Manipulating proteins with chemistry: A cross-section of chemical biology
    • Hahn M.E., and Muir T.W. Manipulating proteins with chemistry: a cross-section of chemical biology Trends Biochem. Sci. 30 2005 26 34
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 26-34
    • Hahn, M.E.1    Muir, T.W.2
  • 6
    • 33746709994 scopus 로고    scopus 로고
    • Cutting out the middle man
    • Muir T.W. Cutting out the middle man Nature 442 2006 517 518
    • (2006) Nature , vol.442 , pp. 517-518
    • Muir, T.W.1
  • 7
    • 29944440968 scopus 로고    scopus 로고
    • Designing split reporter proteins for analytical tools
    • Ozawa T. Designing split reporter proteins for analytical tools Anal. Chim. Acta 556 2006 58 68
    • (2006) Anal. Chim. Acta , vol.556 , pp. 58-68
    • Ozawa, T.1
  • 8
    • 77957758860 scopus 로고    scopus 로고
    • Biological applications of protein splicing
    • Vila-Perello M., and Muir T.W. Biological applications of protein splicing Cell 143 2010 191 200
    • (2010) Cell , vol.143 , pp. 191-200
    • Vila-Perello, M.1    Muir, T.W.2
  • 9
    • 0034665054 scopus 로고    scopus 로고
    • An alternative protein splicing mechanism for inteins lacking an N-terminal nucleophile
    • Southworth M.W., Benner J., and Perler F.B. An alternative protein splicing mechanism for inteins lacking an N-terminal nucleophile EMBO J. 19 2000 5019 5026
    • (2000) EMBO J. , vol.19 , pp. 5019-5026
    • Southworth, M.W.1    Benner, J.2    Perler, F.B.3
  • 10
    • 0942298130 scopus 로고    scopus 로고
    • Protein splicing of inteins with atypical glutamine and aspartate C-terminal residues
    • Amitai G., Dassa B., and Pietrokovski S. Protein splicing of inteins with atypical glutamine and aspartate C-terminal residues J. Biol. Chem. 279 2004 3121 3131
    • (2004) J. Biol. Chem. , vol.279 , pp. 3121-3131
    • Amitai, G.1    Dassa, B.2    Pietrokovski, S.3
  • 11
    • 77249097494 scopus 로고    scopus 로고
    • Splicing of the mycobacteriophage Bethlehem DnaB intein: Identification of a new mechanistic class of inteins that contain an obligate block F nucleophile
    • Tori K., Dassa B., Johnson M.A., Southworth M.W., Brace L.E., and Ishino Y. Splicing of the mycobacteriophage Bethlehem DnaB intein: identification of a new mechanistic class of inteins that contain an obligate block F nucleophile J. Biol. Chem. 285 2010 2515 2526
    • (2010) J. Biol. Chem. , vol.285 , pp. 2515-2526
    • Tori, K.1    Dassa, B.2    Johnson, M.A.3    Southworth, M.W.4    Brace, L.E.5    Ishino, Y.6
  • 12
    • 0027753790 scopus 로고
    • In vitro protein splicing of purified precursor and the identification of a branched intermediate
    • Xu M.Q., Southworth M.W., Mersha F.B., Hornstra L.J., and Perler F.B. In vitro protein splicing of purified precursor and the identification of a branched intermediate Cell 75 1993 1371 1377
    • (1993) Cell , vol.75 , pp. 1371-1377
    • Xu, M.Q.1    Southworth, M.W.2    Mersha, F.B.3    Hornstra, L.J.4    Perler, F.B.5
  • 13
    • 0033782899 scopus 로고    scopus 로고
    • Protein splicing and related forms of protein autoprocessing
    • Paulus H. Protein splicing and related forms of protein autoprocessing Annu. Rev. Biochem. 69 2000 447 496
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 447-496
    • Paulus, H.1
  • 14
    • 0027483414 scopus 로고
    • The curious case of protein splicing: Mechanistic insights suggested by protein semisynthesis
    • Wallace C.J.A. The curious case of protein splicing: mechanistic insights suggested by protein semisynthesis Protein Sci. 2 1993 697 705
    • (1993) Protein Sci. , vol.2 , pp. 697-705
    • Wallace, C.J.A.1
  • 15
    • 0030012109 scopus 로고    scopus 로고
    • Protein splicing: Evidence for an N-O acyl rearrangement as the initial step in the splicing process
    • Shao Y., Xu M.Q., and Paulus H. Protein splicing: evidence for an N-O acyl rearrangement as the initial step in the splicing process Biochemistry 35 1996 3810 3815
    • (1996) Biochemistry , vol.35 , pp. 3810-3815
    • Shao, Y.1    Xu, M.Q.2    Paulus, H.3
  • 16
    • 0027984269 scopus 로고
    • Protein splicing: An analysis of the branched intermediate and its resolution by succinimide formation
    • Xu M.Q., Comb D.G., Paulus H., Noren C.J., Shao Y., and Perler F.B. Protein splicing: an analysis of the branched intermediate and its resolution by succinimide formation EMBO J 13 1994 5517 5522
    • (1994) EMBO J , vol.13 , pp. 5517-5522
    • Xu, M.Q.1    Comb, D.G.2    Paulus, H.3    Noren, C.J.4    Shao, Y.5    Perler, F.B.6
  • 17
    • 0027674383 scopus 로고
    • Protein splicing: Excision of intervening sequences at the protein level
    • Cooper A.A., and Stevens T.H. Protein splicing: excision of intervening sequences at the protein level BioEssays 15 1993 667 674
    • (1993) BioEssays , vol.15 , pp. 667-674
    • Cooper, A.A.1    Stevens, T.H.2
  • 18
    • 0029124041 scopus 로고
    • Protein splicing: Characterization of the aminosuccinimide residue at the carboxyl terminus of the excised intervening sequence
    • Shao Y., Xu M.Q., and Paulus H. Protein splicing: characterization of the aminosuccinimide residue at the carboxyl terminus of the excised intervening sequence Biochemistry 34 1995 10844 10850
    • (1995) Biochemistry , vol.34 , pp. 10844-10850
    • Shao, Y.1    Xu, M.Q.2    Paulus, H.3
  • 19
    • 33847071304 scopus 로고    scopus 로고
    • Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue
    • Van Roey P., Pereira B., Li Z., Hiraga K., Belfort M., and Derbyshire V. Crystallographic and mutational studies of Mycobacterium tuberculosis recA mini-inteins suggest a pivotal role for a highly conserved aspartate residue J. Mol. Biol. 367 2007 162 173
    • (2007) J. Mol. Biol. , vol.367 , pp. 162-173
    • Van Roey, P.1    Pereira, B.2    Li, Z.3    Hiraga, K.4    Belfort, M.5    Derbyshire, V.6
  • 22
    • 79551684493 scopus 로고    scopus 로고
    • Inteins as targets for potential antimycobacterial drugs
    • Paulus H. Inteins as targets for potential antimycobacterial drugs Front. Biosci. 2003 8
    • (2003) Front. Biosci. , pp. 8
    • Paulus, H.1
  • 23
    • 0030803760 scopus 로고    scopus 로고
    • Genetic definition of a protein-splicing domain: Functional mini-inteins support structure predictions and a model for intein evolution
    • Derbyshire V., Wood D.W., Wu W., Dansereau J.T., Dalgaard J.Z., and Belfort M. Genetic definition of a protein-splicing domain: functional mini-inteins support structure predictions and a model for intein evolution Proc. Natl Acad. Sci. USA 94 1997 11466 11471
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 11466-11471
    • Derbyshire, V.1    Wood, D.W.2    Wu, W.3    Dansereau, J.T.4    Dalgaard, J.Z.5    Belfort, M.6
  • 24
    • 0034518359 scopus 로고    scopus 로고
    • Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor
    • Wood D.W., Derbyshire V., Wu W., Chartrain M., Belfort M., and Belfort G. Optimized single-step affinity purification with a self-cleaving intein applied to human acidic fibroblast growth factor Biotechnol. Prog. 16 2000 1055 1063
    • (2000) Biotechnol. Prog. , vol.16 , pp. 1055-1063
    • Wood, D.W.1    Derbyshire, V.2    Wu, W.3    Chartrain, M.4    Belfort, M.5    Belfort, G.6
  • 25
    • 28444477686 scopus 로고    scopus 로고
    • Minimization and stabilization of the Mycobacterium tuberculosis recA intein
    • Hiraga K., Derbyshire V., Dansereau J.T., Van Roey P., and Belfort M. Minimization and stabilization of the Mycobacterium tuberculosis recA intein J. Mol. Biol. 354 2005 916 926
    • (2005) J. Mol. Biol. , vol.354 , pp. 916-926
    • Hiraga, K.1    Derbyshire, V.2    Dansereau, J.T.3    Van Roey, P.4    Belfort, M.5
  • 26
    • 0030763705 scopus 로고    scopus 로고
    • Compilation and analysis of intein sequences
    • Perler F.B., Olsen G.J., and Adam E. Compilation and analysis of intein sequences Nucleic Acids Res. 25 1997 1087 1093
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1087-1093
    • Perler, F.B.1    Olsen, G.J.2    Adam, E.3
  • 27
    • 0031938897 scopus 로고    scopus 로고
    • Modular organization of inteins and C-terminal autocatalytic domains
    • Pietrokovski S. Modular organization of inteins and C-terminal autocatalytic domains Protein Sci. 7 1998 64 71
    • (1998) Protein Sci. , vol.7 , pp. 64-71
    • Pietrokovski, S.1
  • 28
    • 0036084146 scopus 로고    scopus 로고
    • InBase: The Intein Database
    • Perler F.B. InBase: the Intein Database Nucleic Acid Res. 30 2002 383 384 http://www.neb.com/neb/inteins.html Updated July 21, 2010
    • (2002) Nucleic Acid Res. , vol.30 , pp. 383-384
    • Perler, F.B.1
  • 29
    • 0141755113 scopus 로고    scopus 로고
    • Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing
    • Ding Y., Xu M.Q., Ghosh I., Chen X., Ferrandon S., Lesage G., and Rao Z. Crystal structure of a mini-intein reveals a conserved catalytic module involved in side chain cyclization of asparagine during protein splicing J. Biol. Chem. 278 2003 39133 39142
    • (2003) J. Biol. Chem. , vol.278 , pp. 39133-39142
    • Ding, Y.1    Xu, M.Q.2    Ghosh, I.3    Chen, X.4    Ferrandon, S.5    Lesage, G.6    Rao, Z.7
  • 31
    • 0037881919 scopus 로고    scopus 로고
    • Zinc ion effects on individual Ssp DnaE intein splicing steps: Regulating pathway progression
    • Nichols N.M., Benner J.S., Martin D.D., and Evans T.C.J. Zinc ion effects on individual Ssp DnaE intein splicing steps: regulating pathway progression Biochemistry 42 2003 5301 5311
    • (2003) Biochemistry , vol.42 , pp. 5301-5311
    • Nichols, N.M.1    Benner, J.S.2    Martin, D.D.3    Evans, T.C.J.4
  • 32
    • 60349127442 scopus 로고    scopus 로고
    • QM/MM methods for biomolecular systems
    • Senn H.M., and Thiel W. QM/MM methods for biomolecular systems Angew. Chem., Int. Ed. Engl. 48 2009 1198 1229
    • (2009) Angew. Chem., Int. Ed. Engl. , vol.48 , pp. 1198-1229
    • Senn, H.M.1    Thiel, W.2
  • 33
    • 0041876227 scopus 로고    scopus 로고
    • Computer simulations of enzyme catalysis: Methods, progress, and insights
    • Warshel A. Computer simulations of enzyme catalysis: methods, progress, and insights Annu. Rev. Biophys. Biomol. Struct. 32 2003 425 443
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 425-443
    • Warshel, A.1
  • 34
    • 33846570818 scopus 로고    scopus 로고
    • QM/MM: What have we learned, where are we, and where do we go from here?
    • Lin H., and Truhlar D.G. QM/MM: what have we learned, where are we, and where do we go from here? Theor. Chem. Acc. 117 2007 185 199
    • (2007) Theor. Chem. Acc. , vol.117 , pp. 185-199
    • Lin, H.1    Truhlar, D.G.2
  • 35
    • 0000151568 scopus 로고
    • Excited states of the bacteriochlorophyll b dimer of Rhodopseudomonas viridis: A QM/MM study of the photosynthetic reaction center that includes MM polarization
    • Thompson M.A., and Schenter G.K. Excited states of the bacteriochlorophyll b dimer of Rhodopseudomonas viridis: a QM/MM study of the photosynthetic reaction center that includes MM polarization J. Phys. Chem. 99 1995 6374 6386
    • (1995) J. Phys. Chem. , vol.99 , pp. 6374-6386
    • Thompson, M.A.1    Schenter, G.K.2
  • 36
    • 0037055032 scopus 로고    scopus 로고
    • The elusive oxidant species of cytochrome P450 enzymes: Characterization by combined quantum mechanical/molecular mechanical (QM/MM) calculations
    • Schoneboom J.C., Lin H., Reuter N., Thiel W., Cohen S., Ogliaro F., and Shaik S. The elusive oxidant species of cytochrome P450 enzymes: characterization by combined quantum mechanical/molecular mechanical (QM/MM) calculations J. Am. Chem. Soc. 124 2002 8142 8151
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8142-8151
    • Schoneboom, J.C.1    Lin, H.2    Reuter, N.3    Thiel, W.4    Cohen, S.5    Ogliaro, F.6    Shaik, S.7
  • 37
    • 0036025446 scopus 로고    scopus 로고
    • Quantum mechanical methods for enzyme kinetics
    • Gao J., and Truhlar D.G. Quantum mechanical methods for enzyme kinetics Annu. Rev. Phys. Chem. 53 2002 467 505
    • (2002) Annu. Rev. Phys. Chem. , vol.53 , pp. 467-505
    • Gao, J.1    Truhlar, D.G.2
  • 38
    • 0037076062 scopus 로고    scopus 로고
    • A theoretical analysis of the proton and hydride transfer in liver alcohol dehydrogenase (LADH)
    • Cui Q., Elstner M., and Karplus M. A theoretical analysis of the proton and hydride transfer in liver alcohol dehydrogenase (LADH) J. Phys. Chem. B 106 2002 2721 2740
    • (2002) J. Phys. Chem. B , vol.106 , pp. 2721-2740
    • Cui, Q.1    Elstner, M.2    Karplus, M.3
  • 39
    • 0037116512 scopus 로고    scopus 로고
    • Effects of the protein environment on the structure and energetics of active sites of metalloenzymes. ONIOM study of methane monoxygenase and ribonucleotide reductase
    • Torrent M., Vrenen T., Musaev D.G., Morokuma K., Farkas O., and Schlegel H.B. Effects of the protein environment on the structure and energetics of active sites of metalloenzymes. ONIOM study of methane monoxygenase and ribonucleotide reductase J. Am. Chem. Soc. 124 2002 192 193
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 192-193
    • Torrent, M.1    Vrenen, T.2    Musaev, D.G.3    Morokuma, K.4    Farkas, O.5    Schlegel, H.B.6
  • 44
    • 2542452214 scopus 로고    scopus 로고
    • Kluwer Academic/Plenum Publishers New York, Boston, Dordecht, London, Moscow
    • Leskovac V. Comprehensive Enzyme Kinetics 2003 Kluwer Academic/Plenum Publishers New York, Boston, Dordecht, London, Moscow 1 10
    • (2003) Comprehensive Enzyme Kinetics , pp. 1-10
    • Leskovac, V.1
  • 45
    • 3242694003 scopus 로고    scopus 로고
    • Directed evolution of ligand dependence: Small-molecule-activated protein splicing
    • Buskirk A.R., Ong Y.C., Gartner Z.J., and Liu D.R. Directed evolution of ligand dependence: small-molecule-activated protein splicing Proc. Natl Acad. Sci. USA 101 2004 10505 105104
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 10505-105104
    • Buskirk, A.R.1    Ong, Y.C.2    Gartner, Z.J.3    Liu, D.R.4
  • 46
    • 13244252218 scopus 로고    scopus 로고
    • Regulation of protein activity with small-molecule-controlled inteins
    • Skretas G., and Wood D.W. Regulation of protein activity with small-molecule-controlled inteins Protein Sci. 14 2005 523 532
    • (2005) Protein Sci. , vol.14 , pp. 523-532
    • Skretas, G.1    Wood, D.W.2
  • 47
    • 34447525386 scopus 로고    scopus 로고
    • Engineered chimeric enzymes as tools for drug discovery: Generating reliable bacterial screens for the detection, discovery, and assessment of estrogen receptor modulators
    • Skretas G., Meligova A.K., Villalonga-Barber C., Mitsiou D.J., Alexis M.N., and Micha-Screttas M. Engineered chimeric enzymes as tools for drug discovery: generating reliable bacterial screens for the detection, discovery, and assessment of estrogen receptor modulators J. Am. Chem. Soc. 129 2007 8443 8457
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 8443-8457
    • Skretas, G.1    Meligova, A.K.2    Villalonga-Barber, C.3    Mitsiou, D.J.4    Alexis, M.N.5    Micha-Screttas, M.6
  • 48
    • 77953806959 scopus 로고    scopus 로고
    • Branched intermediate formation stimulates peptide bond cleavage in protein splicing
    • Frutos E.A., Goger M., Giovani B., Cowburn D., and Muir T.W. Branched intermediate formation stimulates peptide bond cleavage in protein splicing Nat. Chem. Biol. 6 2010 527 533
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 527-533
    • Frutos, E.A.1    Goger, M.2    Giovani, B.3    Cowburn, D.4    Muir, T.W.5
  • 49
    • 0034162693 scopus 로고    scopus 로고
    • Reactivity of the cysteine residues in the protein splicing active center of the Mycobacterium tuberculosis RecA intein
    • Shingledecker K., Jiang S., and Paulus H. Reactivity of the cysteine residues in the protein splicing active center of the Mycobacterium tuberculosis RecA intein Arch. Biochem. Biophys. 375 2000 138 144
    • (2000) Arch. Biochem. Biophys. , vol.375 , pp. 138-144
    • Shingledecker, K.1    Jiang, S.2    Paulus, H.3
  • 50
    • 77950978248 scopus 로고    scopus 로고
    • Structure and function of factor XI
    • Emsley, J., McEwan, P. A. & Gailani, D., Structure and function of factor XI. Blood 115, 2569 - 2577.
    • Blood , vol.115 , pp. 2569-2577
    • Emsley, J.1    McEwan, P.A.2    Gailani, D.3
  • 51
    • 0033548087 scopus 로고    scopus 로고
    • Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis
    • Kishi T., Kato M., Shimizu T., Kato K., Matsumoto K., and Yoshida S. Crystal structure of neuropsin, a hippocampal protease involved in kindling epileptogenesis J. Biol. Chem. 274 1999 4220 4224
    • (1999) J. Biol. Chem. , vol.274 , pp. 4220-4224
    • Kishi, T.1    Kato, M.2    Shimizu, T.3    Kato, K.4    Matsumoto, K.5    Yoshida, S.6
  • 52
    • 36048940448 scopus 로고    scopus 로고
    • Chymotryptic specificity determinants in the 1.0 C structure of the zinc-inhibited human tissue kallikrein 7
    • Debela M., Hess P., Magdolen V., Schechter N.M., Steiner T., and Huber R. Chymotryptic specificity determinants in the 1.0 C structure of the zinc-inhibited human tissue kallikrein 7 Proc. Natl Acad. Sci. USA 104 2007 16086 16091
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16086-16091
    • Debela, M.1    Hess, P.2    Magdolen, V.3    Schechter, N.M.4    Steiner, T.5    Huber, R.6
  • 53
    • 0028586082 scopus 로고
    • The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: Changes accompanying activation and exosite binding to thrombin
    • Vijayalakshmi J., Padmanabhan K.P., Mann K.G., and Tulinsky A. The isomorphous structures of prethrombin2, hirugen-, and PPACK-thrombin: changes accompanying activation and exosite binding to thrombin Protein Sci. 3 1994 2254 2271
    • (1994) Protein Sci. , vol.3 , pp. 2254-2271
    • Vijayalakshmi, J.1    Padmanabhan, K.P.2    Mann, K.G.3    Tulinsky, A.4
  • 54
    • 0037112699 scopus 로고    scopus 로고
    • Intein-mediated purification of cytotoxic endonuclease I-TevI by insertional inactivation and pH-controllable splicing
    • Wu W., Wood D.W., Belfort G., Derbyshire V., and Belfort M. Intein-mediated purification of cytotoxic endonuclease I-TevI by insertional inactivation and pH-controllable splicing Nucleic Acids Res. 30 2002 4864 4871
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4864-4871
    • Wu, W.1    Wood, D.W.2    Belfort, G.3    Derbyshire, V.4    Belfort, M.5
  • 55
    • 0025990865 scopus 로고
    • Novel structure of the RecA locus of Mycobacterium tuberculosis implies processing of the gene product
    • Davis E.O., Sedgwick S.G., and Colston M.J. Novel structure of the RecA locus of Mycobacterium tuberculosis implies processing of the gene product J. Bacteriol. 173 1991 5653 5662
    • (1991) J. Bacteriol. , vol.173 , pp. 5653-5662
    • Davis, E.O.1    Sedgwick, S.G.2    Colston, M.J.3
  • 56
    • 0031556945 scopus 로고    scopus 로고
    • Two-domain structure of the td intron-encoded endonuclease I-TevI correlates with the two-domain configuration of the homing site
    • Derbyshire V., Kowalski J.C., Dansereau J.T., Hauer C.R., and Belfort M. Two-domain structure of the td intron-encoded endonuclease I-TevI correlates with the two-domain configuration of the homing site J. Mol. Biol. 265 1997 494 506
    • (1997) J. Mol. Biol. , vol.265 , pp. 494-506
    • Derbyshire, V.1    Kowalski, J.C.2    Dansereau, J.T.3    Hauer, C.R.4    Belfort, M.5
  • 57
    • 84986527758 scopus 로고
    • IMOMM-a new integrated ab initio plus molecular mechanics geometry optimization scheme of equilibrium structures and transition states
    • Maseras F., and Morokuma K. IMOMM-a new integrated ab initio plus molecular mechanics geometry optimization scheme of equilibrium structures and transition states J. Comput. Chem. 16 1995 1170 1179
    • (1995) J. Comput. Chem. , vol.16 , pp. 1170-1179
    • Maseras, F.1    Morokuma, K.2
  • 58
    • 0037473497 scopus 로고    scopus 로고
    • Geometry optimization with QM/MM, ONIOM, and other combined methods. I. Microiterations and constraints
    • Vreven T., Morokuma K., Farkas O., Schlegel H.B., and Frisch M.J. Geometry optimization with QM/MM, ONIOM, and other combined methods. I. Microiterations and constraints J. Comput. Chem. 24 2003 760 769
    • (2003) J. Comput. Chem. , vol.24 , pp. 760-769
    • Vreven, T.1    Morokuma, K.2    Farkas, O.3    Schlegel, H.B.4    Frisch, M.J.5
  • 59
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke A.D. Density-functional thermochemistry. III. The role of exact exchange J. Chem. Phys. 98 1993 5648 5652
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 60
    • 0347170005 scopus 로고
    • Self-consistent molecular orbital methods. XII. Further extensions of Gaussian-type basis sets for use in molecular orbital studies of organic molecules
    • Hehre W.J., Ditchfield R., and Pople J.A. Self-consistent molecular orbital methods. XII. Further extensions of Gaussian-type basis sets for use in molecular orbital studies of organic molecules J. Chem. Phys. 56 1972 2257 2261
    • (1972) J. Chem. Phys. , vol.56 , pp. 2257-2261
    • Hehre, W.J.1    Ditchfield, R.2    Pople, J.A.3
  • 61
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • Cornell W.D., Cieplak P., Bayley C.I., Gould I.R., Merz K.M., and Ferguson D.M. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules J. Am. Chem. Soc. 117 1995 5179 5197
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    Cieplak, P.2    Bayley, C.I.3    Gould, I.R.4    Merz, K.M.5    Ferguson, D.M.6
  • 62
    • 33748365234 scopus 로고    scopus 로고
    • Transition state theory can be used in studies of enzyme catalysis: Lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems
    • Olsson M.H., Mavri J., and Warshel A. Transition state theory can be used in studies of enzyme catalysis: lessons from simulations of tunnelling and dynamical effects in lipoxygenase and other systems Philos. Trans. R. Soc. London, Ser. B 361 2006 1417 1432
    • (2006) Philos. Trans. R. Soc. London, Ser. B , vol.361 , pp. 1417-1432
    • Olsson, M.H.1    Mavri, J.2    Warshel, A.3


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