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Volumn 29, Issue 2, 2003, Pages 185-192

The first semi-synthetic serine protease made by native chemical ligation

Author keywords

[No Author keywords available]

Indexed keywords

STREPTOMYCES; STREPTOMYCES GRISEUS;

EID: 0037791019     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(03)00022-6     Document Type: Article
Times cited : (15)

References (53)
  • 1
    • 0023889559 scopus 로고
    • Chemical synthesis of peptides and proteins
    • S.B. Kent, Chemical synthesis of peptides and proteins, Annu. Rev Biochem. 57 (1988) 957-989.
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 957-989
    • Kent, S.B.1
  • 3
    • 0026686436 scopus 로고
    • Total chemical synthesis of a D-enzyme: The enantiomers of HIV-1 protease show reciprocal chiral substrate specificity
    • R.C. Milton, S.C. Milton, S.B. Kent, Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected], Science 256 (1992) 1445-1448.
    • (1992) Science , vol.256 , pp. 1445-1448
    • Milton, R.C.1    Milton, S.C.2    Kent, S.B.3
  • 4
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • C.J. Noren, S.J. Anthony_Cahill, M.C. Griffith, P.G. Schultz, A general method for site-specific incorporation of unnatural amino acids into proteins, Science 244 (1989) 182-188.
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 6
    • 0026523058 scopus 로고
    • Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code
    • J.D. Bain, C. Switzer, A.R. Chamberlin, S.A. Benner, Ribosome-mediated incorporation of a non-standard amino acid into a peptide through expansion of the genetic code, Nature 356 (1992) 537-539.
    • (1992) Nature , vol.356 , pp. 537-539
    • Bain, J.D.1    Switzer, C.2    Chamberlin, A.R.3    Benner, S.A.4
  • 7
    • 0029982453 scopus 로고    scopus 로고
    • Incorporation of an unnatural amino acid in the active site of porcine pancreatic phospholipase A2. Substitution of histidine by 1,2,4-triazole-3-alanine yields an enzyme with high activity at acidic pH
    • S.H. Beiboer, B. van_den_Berg, N. Dekker, R.C. Cox, H.M. Verheij, Incorporation of an unnatural amino acid in the active site of porcine pancreatic phospholipase A2. Substitution of histidine by 1,2,4-triazole-3-alanine yields an enzyme with high activity at acidic pH, Protein Eng. 9 (1996) 345-352.
    • (1996) Protein Eng. , vol.9 , pp. 345-352
    • Beiboer, S.H.1    Van Den Berg, B.2    Dekker, N.3    Cox, R.C.4    Verheij, H.M.5
  • 8
    • 0032928678 scopus 로고    scopus 로고
    • Toward the experimental codon reassignment in vivo: Protein building with an expanded amino acid repertoire
    • N. Budisa, C. Minks, S. Alefelder, W. Wenger, F. Dong, L. Moroder, R. Huber, Toward the experimental codon reassignment in vivo: protein building with an expanded amino acid repertoire, FASEB J. 13 (1999) 41-51.
    • (1999) FASEB J. , vol.13 , pp. 41-51
    • Budisa, N.1    Minks, C.2    Alefelder, S.3    Wenger, W.4    Dong, F.5    Moroder, L.6    Huber, R.7
  • 9
    • 0034704064 scopus 로고    scopus 로고
    • A mutant Escherichia coli tyrosyl-tRNA synthetase utilizes the unnatural amino acid azatyrosine more efficiently than tyrosine
    • F. Hamano_Takaku, T. Iwama, S. Saito_Yano, K. Takaku, Y. Monden, M. Kitabatake, D. Soll, S. Nishimura, A mutant Escherichia coli tyrosyl-tRNA synthetase utilizes the unnatural amino acid azatyrosine more efficiently than tyrosine. J. Biol. Chem. 275 (2000) 40324-40328.
    • (2000) J. Biol. Chem. , vol.275 , pp. 40324-40328
    • Hamano Takaku, F.1    Iwama, T.2    Saito Yano, S.3    Takaku, K.4    Monden, Y.5    Kitabatake, M.6    Soll, D.7    Nishimura, S.8
  • 10
    • 0034003659 scopus 로고    scopus 로고
    • Efficient incorporation of unsaturated methionine analogues into proteins in vivo
    • J.C.M. van Hest, K.L. Kiick, D.A. Tirrell, Efficient incorporation of unsaturated methionine analogues into proteins in vivo, J. Am. Chem. Soc. 122 (2000) 1282-1288.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 1282-1288
    • Van Hest, J.C.M.1    Kiick, K.L.2    Tirrell, D.A.3
  • 11
    • 0027412820 scopus 로고
    • Binding of amino acid side chains to preformed cavities: Interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues
    • T.L. Bigler, W. Lu, S.J. Park, M. Tashiro, M. Wieczorek, R. Wynn, M. Laskowski, Binding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues, Protein Sci. 2 (1993) 786-799.
    • (1993) Protein Sci. , vol.2 , pp. 786-799
    • Bigler, T.L.1    Lu, W.2    Park, S.J.3    Tashiro, M.4    Wieczorek, M.5    Wynn, R.6    Laskowski, M.7
  • 12
    • 0028518514 scopus 로고
    • A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues
    • D.Y. Jackson, J. Burnier, C. Quan, M. Stanley, J. Tom, J.A. Wells, A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues, Science 266 (1994) 243-247.
    • (1994) Science , vol.266 , pp. 243-247
    • Jackson, D.Y.1    Burnier, J.2    Quan, C.3    Stanley, M.4    Tom, J.5    Wells, J.A.6
  • 13
    • 0029102380 scopus 로고
    • Peptide ligation and semisynthesis
    • C.J. Wallace, Peptide ligation and semisynthesis, Curr. Opin. Biotechnol. 6 (1995) 403-410.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 403-410
    • Wallace, C.J.1
  • 14
    • 0027944205 scopus 로고
    • Synthesis of proteins by native chemical ligation
    • P.E. Dawson, T.W. Muir, I. Clark_Lewis, S.B. Kent, Synthesis of proteins by native chemical ligation, Science 266 (1994) 776-779.
    • (1994) Science , vol.266 , pp. 776-779
    • Dawson, P.E.1    Muir, T.W.2    Clark Lewis, I.3    Kent, S.B.4
  • 15
    • 0033791223 scopus 로고    scopus 로고
    • Synthesis of native proteins by chemical ligation
    • P.E. Dawson, S.B. Kent, Synthesis of native proteins by chemical ligation, Annu. Rev. Biochem 69 (2000) 923-960.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 923-960
    • Dawson, P.E.1    Kent, S.B.2
  • 16
    • 0035811061 scopus 로고    scopus 로고
    • Total synthesis of cytochrome b562 by native chemical ligation using a removable auxiliary
    • D.W. Low, M.G. Hill, M.R. Carrasco, S.B. Kent, P. Botti, Total synthesis of cytochrome b562 by native chemical ligation using a removable auxiliary, Proc. Natl. Acad. Sci. USA 98 (2001) 6554-6559.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6554-6559
    • Low, D.W.1    Hill, M.G.2    Carrasco, M.R.3    Kent, S.B.4    Botti, P.5
  • 17
    • 0029559773 scopus 로고
    • Peptide synthesis using unprotected peptides through orthogonal coupling methods
    • J.P. Tam, Y.A. Lu, C.F. Liu, J. Shao, Peptide synthesis using unprotected peptides through orthogonal coupling methods, Proc. Natl. Acad. Sci. USA 92 (1995) 12485-12489.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 12485-12489
    • Tam, J.P.1    Lu, Y.A.2    Liu, C.F.3    Shao, J.4
  • 18
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • L. Wang, A. Brock, B. Herberich, P.G. Schultz, Expanding the genetic code of Escherichia coli, Science 292 (2001) 498-500.
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 19
    • 0037028931 scopus 로고    scopus 로고
    • Adding L-3-(2-naphthyl)alanine to the genetic code of E. coli
    • L. Wang, A. Brock, P.G. Schultz, Adding L-3-(2-naphthyl)alanine to the genetic code of E. coli, J. Am. Chem. Soc. 124 (2002) 1836-1837.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1836-1837
    • Wang, L.1    Brock, A.2    Schultz, P.G.3
  • 20
    • 0033615313 scopus 로고    scopus 로고
    • Chemical protein synthesis by solid phase ligation of unprotected peptide segments
    • L.E. Canne, P. Botti, R.J. Simon, Y. Chen, E.A. Dennis, S.B. Kent, Chemical protein synthesis by solid phase ligation of unprotected peptide segments, J. Am. Chem. Soc. 121 (1999) 8720-8727.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8720-8727
    • Canne, L.E.1    Botti, P.2    Simon, R.J.3    Chen, Y.4    Dennis, E.A.5    Kent, S.B.6
  • 21
    • 0032499752 scopus 로고    scopus 로고
    • Expressed protein ligation: A general method for protein engineering
    • T.W. Muir, D. Sondhi, P.A. Cole, Expressed protein ligation: a general method for protein engineering, Proc. Natl. Acad. Sci. USA 95 (1998) 6705-6710.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6705-6710
    • Muir, T.W.1    Sondhi, D.2    Cole, P.A.3
  • 22
    • 0033200393 scopus 로고    scopus 로고
    • Peptide ligation and its application to protein engineering
    • G.J. Cotton, T.W. Muir, Peptide ligation and its application to protein engineering, Chem. Biol. 6 (1999) R247-R256.
    • (1999) Chem. Biol. , vol.6
    • Cotton, G.J.1    Muir, T.W.2
  • 23
    • 0034177596 scopus 로고    scopus 로고
    • Generation of a dual-labeled fluorescence biosensor for Crk-II phosphorylation using solid-phase expressed protein ligation
    • G.J. Cotton, T.W. Muir, Generation of a dual-labeled fluorescence biosensor for Crk-II phosphorylation using solid-phase expressed protein ligation, Chem. Biol. 7 (2000) 253-261.
    • (2000) Chem. Biol. , vol.7 , pp. 253-261
    • Cotton, G.J.1    Muir, T.W.2
  • 24
    • 0033582287 scopus 로고    scopus 로고
    • Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
    • R. Xu, B. Ayers, D. Cowburn, T.W. Muir, Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies, Proc. Natl. Acad. Sci. USA 96 (1999) 388-393.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 388-393
    • Xu, R.1    Ayers, B.2    Cowburn, D.3    Muir, T.W.4
  • 25
    • 0034177836 scopus 로고    scopus 로고
    • Biosynthetic phage display: A novel protein engineering tool combining chemical and genetic diversity
    • M.A. Dwyer, W. Lu, J.J. Dwyer, A.A. Kossiakoff, Biosynthetic phage display: a novel protein engineering tool combining chemical and genetic diversity, Chem. Biol. 7 (2000) 263-274.
    • (2000) Chem. Biol. , vol.7 , pp. 263-274
    • Dwyer, M.A.1    Lu, W.2    Dwyer, J.J.3    Kossiakoff, A.A.4
  • 27
    • 0023384982 scopus 로고
    • Engineering enzyme specificity by "substrate-assisted catalysis"
    • P. Carter, J.A. Wells, Engineering enzyme specificity by "substrate-assisted catalysis", Science 237 (1987) 394-399.
    • (1987) Science , vol.237 , pp. 394-399
    • Carter, P.1    Wells, J.A.2
  • 28
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • T.A. Kunkel, J.D. Roberts, R.A. Zakour, Rapid and efficient site-specific mutagenesis without phenotypic selection, Methods Enzymol. 154 (1987) 367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 29
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • M. Schnolzer, P. Alewood, A. Jones, D. Alewood, S.B. Kent, In situ neutralization in Boc-chemistry solid phase peptide synthesis. Rapid, high yield assembly of difficult sequences, Int. J. Pept. Protein Res. 40 (1992) 180-193.
    • (1992) Int. J. Pept. Protein Res. , vol.40 , pp. 180-193
    • Schnolzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.5
  • 31
    • 0033033272 scopus 로고    scopus 로고
    • High performance in refolding of Streptomyces griseus trypsin by the aid of a mutant of Streptomyces subtilisin inhibitor designed as trypsin inhibitor
    • D. Nohara, H. Sugiura, H. Sakakibara, M. Matsubara, S. Kojima, K. Miura, T. Sakai, High performance in refolding of Streptomyces griseus trypsin by the aid of a mutant of Streptomyces subtilisin inhibitor designed as trypsin inhibitor, J. Biochem. 125 (1999) 343-347.
    • (1999) J. Biochem. , vol.125 , pp. 343-347
    • Nohara, D.1    Sugiura, H.2    Sakakibara, H.3    Matsubara, M.4    Kojima, S.5    Miura, K.6    Sakai, T.7
  • 32
    • 0344815737 scopus 로고
    • Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid
    • P.H. Hirel, M.J. Schmitter, P. Dessen, G. Fayat, S. Blanquet, Extent of N-terminal methionine excision from Escherichia coli proteins is governed by the side-chain length of the penultimate amino acid, Proc. Natl. Acad. Sci. USA 86 (1989) 8247-8251.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 8247-8251
    • Hirel, P.H.1    Schmitter, M.J.2    Dessen, P.3    Fayat, G.4    Blanquet, S.5
  • 33
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • F. Baneyx, Recombinant protein expression in Escherichia coli, Curr. Opin. Biotechnol. 10 (1999) 411-421.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 34
    • 0033537948 scopus 로고    scopus 로고
    • Translational enhancement by an element downstream of the initiation codon in Escherichia coli
    • J.P. Etchegaray, M. Inouye, Translational enhancement by an element downstream of the initiation codon in Escherichia coli, J. Biol. Chem. 274 (1999) 10079-10085.
    • (1999) J. Biol. Chem. , vol.274 , pp. 10079-10085
    • Etchegaray, J.P.1    Inouye, M.2
  • 35
    • 0023881841 scopus 로고
    • Refined crystal structure of Streptomyces griseus trypsin at 1.7A resolution
    • R.J. Read, M.N. James, Refined crystal structure of Streptomyces griseus trypsin at 1.7A resolution, J. Mol. Biol. 200 (1988) 523-551.
    • (1988) J. Mol. Biol. , vol.200 , pp. 523-551
    • Read, R.J.1    James, M.N.2
  • 36
    • 0025005525 scopus 로고
    • Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease
    • D. Shortle, W.E. Stites, A.K. Meeker, Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease, Biochemistry 29 (1990) 8033-8041.
    • (1990) Biochemistry , vol.29 , pp. 8033-8041
    • Shortle, D.1    Stites, W.E.2    Meeker, A.K.3
  • 37
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • L. Serrano, J.T. Kellis, P. Cann, A. Matouschek, A.R. Fersht, The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability, J. Mol. Biol. 224 (1992) 783-804.
    • (1992) J. Mol. Biol. , vol.224 , pp. 783-804
    • Serrano, L.1    Kellis, J.T.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 38
    • 0027991944 scopus 로고
    • Thermodynamic and structural consequences of changing a sulfur atom to a methylene group in the M13Nle mutation in ribonuclease-S
    • J. Thomson, G.S. Ratnaparkhi, R. Varadarajan, J.M. Sturtevant, F.M. Richards, Thermodynamic and structural consequences of changing a sulfur atom to a methylene group in the M13Nle mutation in ribonuclease-S, Biochemistry 33 (1994) 8587-8593.
    • (1994) Biochemistry , vol.33 , pp. 8587-8593
    • Thomson, J.1    Ratnaparkhi, G.S.2    Varadarajan, R.3    Sturtevant, J.M.4    Richards, F.M.5
  • 39
    • 0028968018 scopus 로고
    • Studies on protein stability with T4 lysozyme
    • B.W. Matthews, Studies on protein stability with T4 lysozyme, Adv. Protein Chem. 46 (1995) 249-278.
    • (1995) Adv. Protein Chem. , vol.46 , pp. 249-278
    • Matthews, B.W.1
  • 42
    • 0032953154 scopus 로고    scopus 로고
    • Enhancement of cyanogen bromide cleavage yields for methionyl-serine and methionyl-threonine peptide bonds
    • R. Kaiser, L. Metzka, Enhancement of cyanogen bromide cleavage yields for methionyl-serine and methionyl-threonine peptide bonds, Anal. Biochem. 266 (1999) 1-8.
    • (1999) Anal. Biochem. , vol.266 , pp. 1-8
    • Kaiser, R.1    Metzka, L.2
  • 43
    • 0018378575 scopus 로고
    • Partial non-cleavage by cyanogen bromide of a methionine-cystine bond from human serum albumin and bovine alpha-lactalbumin
    • N. Doyen, C Lapresle, Partial non-cleavage by cyanogen bromide of a methionine-cystine bond from human serum albumin and bovine alpha-lactalbumin, Biochem. J. 177 (1979) 251-254.
    • (1979) Biochem. J. , vol.177 , pp. 251-254
    • Doyen, N.1    Lapresle, C.2
  • 44
    • 0025356855 scopus 로고
    • Formylated peptides from cyanogen bromide digests identified by fast atom bombardment mass spectrometry
    • D.R. Goodlett, F.B. Armstrong, R.J. Creech, R.B. van_Breemen, Formylated peptides from cyanogen bromide digests identified by fast atom bombardment mass spectrometry, Anal. Biochem. 186 (1990) 116-120.
    • (1990) Anal. Biochem. , vol.186 , pp. 116-120
    • Goodlett, D.R.1    Armstrong, F.B.2    Creech, R.J.3    Van Breemen, R.B.4
  • 45
    • 54749104992 scopus 로고    scopus 로고
    • CNBr/formic acid reactions of methionine- and trifluoromethionine-containing λ lysozyme: Probing chemical and positional reactivity and formylation side reactions by mass spectrometry
    • H.S. Duewel, J.F. Honek, CNBr/formic acid reactions of methionine- and trifluoromethionine-containing λ lysozyme: probing chemical and positional reactivity and formylation side reactions by mass spectrometry, J. Protein Chem. 17 (1998) 337-350.
    • (1998) J. Protein Chem. , vol.17 , pp. 337-350
    • Duewel, H.S.1    Honek, J.F.2
  • 46
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • J.J. Perona, C.S. Craik, Structural basis of substrate specificity in the serine proteases, Protein Sci. 4 (1995) 337-360.
    • (1995) Protein Sci. , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 47
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold
    • J.J. Perona, C.S. Craik, Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold, J. Biol. Chem. 272 (1997) 29987-29990.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29987-29990
    • Perona, J.J.1    Craik, C.S.2
  • 48
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • G. Dodson, A. Wlodawer, Catalytic triads and their relatives, Trends Biochem. Sci. 23 (1998) 347-352.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 49
    • 0028040716 scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases
    • P.A. Frey, S.A. Whitt, J.B. Tobin, A low-barrier hydrogen bond in the catalytic triad of serine proteases, Science 264 (1994) 1927-1930.
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3
  • 50
    • 0030723218 scopus 로고    scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment
    • E.L. Ash, J.L. Sudmeier, E.C. De_Fabo, W.W. Bachovchin, A low-barrier hydrogen bond in the catalytic triad of serine proteases?. Theory versus experiment, Science 278 (1997) 1128-1132.
    • (1997) Science , vol.278 , pp. 1128-1132
    • Ash, E.L.1    Sudmeier, J.L.2    De Fabo, E.C.3    Bachovchin, W.W.4
  • 51
    • 0032475836 scopus 로고    scopus 로고
    • The low barrier hydrogen bond in enzymatic catalysis
    • W.W. Cleland, P.A. Frey, J.A. Gerlt, The low barrier hydrogen bond in enzymatic catalysis, J. Biol. Chem. 273 (1998) 25529-25532.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25529-25532
    • Cleland, W.W.1    Frey, P.A.2    Gerlt, J.A.3
  • 52
    • 0032538627 scopus 로고    scopus 로고
    • Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites
    • A. Warshel, Electrostatic origin of the catalytic power of enzymes and the role of preorganized active sites, J. Biol. Chem. 273 (1998) 27035-27038.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27035-27038
    • Warshel, A.1
  • 53
    • 0030462453 scopus 로고    scopus 로고
    • Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds
    • A. Warshel, A. Papazyan, Energy considerations show that low-barrier hydrogen bonds do not offer a catalytic advantage over ordinary hydrogen bonds, Proc. Natl. Acad. Sci. USA 93 (1996) 13665-13670.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 13665-13670
    • Warshel, A.1    Papazyan, A.2


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