메뉴 건너뛰기




Volumn 76, Issue 3, 1999, Pages 1571-1579

His ··· Asp catalytic dyad of ribonuclease A: Histidine pK(a) values in the wild-type, D121N, and D121A enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; HISTIDINE; PANCREATIC RIBONUCLEASE; URIDINE PHOSPHATE; LIGAND;

EID: 0032589144     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(99)77316-9     Document Type: Article
Times cited : (50)

References (58)
  • 2
    • 0030723218 scopus 로고    scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment
    • Ash, E. L., J. L. Sudmeier, E. C. De Fabo, and W. W. Bachovchin. 1997. A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment. Science. 278:1128-1132.
    • (1997) Science , vol.278 , pp. 1128-1132
    • Ash, E.L.1    Sudmeier, J.L.2    De Fabo, E.C.3    Bachovchin, W.W.4
  • 3
    • 0008011643 scopus 로고
    • Structure, properties and molecular evolution of pancreatic-type ribonucleases
    • Beintema, J. J. 1987. Structure, properties and molecular evolution of pancreatic-type ribonucleases. Life Chem. Rep. 4:333-389.
    • (1987) Life Chem. Rep. , vol.4 , pp. 333-389
    • Beintema, J.J.1
  • 5
    • 0344887064 scopus 로고
    • Equilibrium acidities in dimethyl sulfoxide solution
    • Bordwell, F. G. 1988. Equilibrium acidities in dimethyl sulfoxide solution. Acc. Chem. Res. 21:456-463.
    • (1988) Acc. Chem. Res. , vol.21 , pp. 456-463
    • Bordwell, F.G.1
  • 6
    • 0001709899 scopus 로고
    • Ribonuclease-A: Least-squares refinement of the structure at 1.45 Å resolution
    • Borkakoti, N., D. S. Moss, and R. A. Palmer. 1982. Ribonuclease-A: least-squares refinement of the structure at 1.45 Å resolution. Acta Crystallogr. B. 38:2210-2217.
    • (1982) Acta Crystallogr. B , vol.38 , pp. 2210-2217
    • Borkakoti, N.1    Moss, D.S.2    Palmer, R.A.3
  • 7
    • 0344904381 scopus 로고
    • 1H-NMR studies of the solution structure of RNase A-pyrimidine-nucleotide complexes
    • R. de Llorens, C. M. Cuchillo, M. V. Nogués, and X. Parés, editors. Universitat Autónoma de Barcelona, Bellaterra, Spain
    • 1H-NMR studies of the solution structure of RNase A-pyrimidine-nucleotide complexes. In Structure, Mechanism and Function of Ribonucleases. R. de Llorens, C. M. Cuchillo, M. V. Nogués, and X. Parés, editors. Universitat Autónoma de Barcelona, Bellaterra, Spain. 15-20.
    • (1991) Structure, Mechanism and Function of Ribonucleases , pp. 15-20
    • Bruix, M.1    Rico, M.2    González, C.3    Neira, J.L.4    Santoro, J.5    Nieto, J.L.6    Rüterjans, H.7
  • 8
    • 0030937806 scopus 로고    scopus 로고
    • A new concept for the mechanism of action of chymotrypsin: The role of the low-barrier hydrogen bond
    • Cassidy, C. S., J. Lin, and P. A. Frey. 1997. A new concept for the mechanism of action of chymotrypsin: the role of the low-barrier hydrogen bond. Biochemistry. 36:4576-4584.
    • (1997) Biochemistry , vol.36 , pp. 4576-4584
    • Cassidy, C.S.1    Lin, J.2    Frey, P.A.3
  • 11
    • 0026544171 scopus 로고
    • Low-barrier hydrogen bonds and low fractionation factor bases in enzymatic reactions
    • Cleland, W. W. 1992. Low-barrier hydrogen bonds and low fractionation factor bases in enzymatic reactions. Biochemistry. 31:317-319.
    • (1992) Biochemistry , vol.31 , pp. 317-319
    • Cleland, W.W.1
  • 12
    • 0028030684 scopus 로고
    • Low-barrier hydrogen bonds and enzymic catalysis
    • Cleland, W. W., and M. M. Kreevoy. 1994. Low-barrier hydrogen bonds and enzymic catalysis. Science. 264:1887-1890.
    • (1994) Science , vol.264 , pp. 1887-1890
    • Cleland, W.W.1    Kreevoy, M.M.2
  • 13
    • 0027430772 scopus 로고
    • The role of 2′,3′-cyclic phosphodiesters in the bovine pancreatic ribonuclease A catalysed cleavage of RNA: Intermediates or products?
    • Cuchillo, C. M., X. Parés, A. Guasch, T. Barman, F. Travers, and M. V. Nogués. 1993. The role of 2′,3′-cyclic phosphodiesters in the bovine pancreatic ribonuclease A catalysed cleavage of RNA: intermediates or products? FEBS Lett. 333:207-210.
    • (1993) FEBS Lett. , vol.333 , pp. 207-210
    • Cuchillo, C.M.1    Parés, X.2    Guasch, A.3    Barman, T.4    Travers, F.5    Nogués, M.V.6
  • 14
    • 0029091002 scopus 로고
    • A residue to residue hydrogen bond mediates the nucleotide specificity of ribonuclease A
    • delCardayré, S. B., and R. T. Raines. 1995. A residue to residue hydrogen bond mediates the nucleotide specificity of ribonuclease A. J. Mol. Biol. 252:328-336.
    • (1995) J. Mol. Biol. , vol.252 , pp. 328-336
    • DelCardayré, S.B.1    Raines, R.T.2
  • 15
    • 0026501884 scopus 로고
    • Structural changes that accompany the reduced catalytic efficiency of two semisynthetic ribonuclease analogs
    • de Mel, V. S. J., P. D. Martin, M. S. Doscher, and B. F. P. Edwards. 1992. Structural changes that accompany the reduced catalytic efficiency of two semisynthetic ribonuclease analogs. J. Biol. Chem. 267:247-256.
    • (1992) J. Biol. Chem. , vol.267 , pp. 247-256
    • De Mel, V.S.J.1    Martin, P.D.2    Doscher, M.S.3    Edwards, B.F.P.4
  • 16
    • 0021112613 scopus 로고
    • Energetics of ribonuclease A catalysis. 1. pH, ionic strength, and solvent isotope dependence of the hydrolysis of cytidine cyclic 2′,3′-phosphate
    • Eftink, M. R., and R. L. Biltonen. 1983. Energetics of ribonuclease A catalysis. 1. pH, ionic strength, and solvent isotope dependence of the hydrolysis of cytidine cyclic 2′,3′-phosphate. Biochemistry. 22: 5123-5134.
    • (1983) Biochemistry , vol.22 , pp. 5123-5134
    • Eftink, M.R.1    Biltonen, R.L.2
  • 18
    • 0000403579 scopus 로고
    • The active site and mechanism of action of bovine pancreatic ribonuclease
    • Findlay, D., D. G. Herries, A. P. Mathias, B. R. Rabin, and C. A. Ross. 1961. The active site and mechanism of action of bovine pancreatic ribonuclease. Nature. 190:781-784.
    • (1961) Nature , vol.190 , pp. 781-784
    • Findlay, D.1    Herries, D.G.2    Mathias, A.P.3    Rabin, B.R.4    Ross, C.A.5
  • 19
    • 0032545388 scopus 로고    scopus 로고
    • A new remote subsite in ribonuclease A
    • Fisher, B. M., J. E. Grilley, and R. T. Raines. 1998a. A new remote subsite in ribonuclease A. J. Biol. Chem. 273:34134-34138.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34134-34138
    • Fisher, B.M.1    Grilley, J.E.2    Raines, R.T.3
  • 20
    • 0032535188 scopus 로고    scopus 로고
    • Coulombic effects of remote subsites on the active site of ribonuclease A
    • Fisher, B. M., L. W. Schultz, and R. T. Raines. 1998b. Coulombic effects of remote subsites on the active site of ribonuclease A. Biochemistry. 37:17386-17401.
    • (1998) Biochemistry , vol.37 , pp. 17386-17401
    • Fisher, B.M.1    Schultz, L.W.2    Raines, R.T.3
  • 21
    • 0016682964 scopus 로고
    • The pH dependence of the thermodynamics of the interaction of 3′-cytidine monophosphate with ribonuclease A
    • Flogel, M., and R. L. Biltonen. 1975. The pH dependence of the thermodynamics of the interaction of 3′-cytidine monophosphate with ribonuclease A. Biochemistry. 14:2610-2615.
    • (1975) Biochemistry , vol.14 , pp. 2610-2615
    • Flogel, M.1    Biltonen, R.L.2
  • 23
    • 0028040716 scopus 로고
    • A low-barrier hydrogen bond in the catalytic triad of serine proteases
    • Frey, P. A., S. A. Whitt, and J. B. Tobin. 1994. A low-barrier hydrogen bond in the catalytic triad of serine proteases. Science. 264:1927-1930.
    • (1994) Science , vol.264 , pp. 1927-1930
    • Frey, P.A.1    Whitt, S.A.2    Tobin, J.B.3
  • 24
    • 0001970541 scopus 로고    scopus 로고
    • Crystallographic studies of ribonuclease complexes
    • G. D'Alessio and J. F. Riordan, editors. Academic Press, New York
    • Gilliland, G. L. 1997. Crystallographic studies of ribonuclease complexes. In Ribonucleases: Structures and Functions. G. D'Alessio and J. F. Riordan, editors. Academic Press, New York. 306-341.
    • (1997) Ribonucleases: Structures and Functions , pp. 306-341
    • Gilliland, G.L.1
  • 25
    • 0344041626 scopus 로고    scopus 로고
    • NMR solution structures of ribonuclease A and its complexes with mono and dinucleotides
    • G. D'Alessio and J. F. Riordan, editors. Academic Press, New York
    • González, C., J. Santoro, and M. Rico. 1997. NMR solution structures of ribonuclease A and its complexes with mono and dinucleotides. In Ribonucleases: Structures and Functions. G. D'Alessio and J. F. Riordan, editors. Academic Press, New York. 343-381.
    • (1997) Ribonucleases: Structures and Functions , pp. 343-381
    • González, C.1    Santoro, J.2    Rico, M.3
  • 26
    • 0015698181 scopus 로고
    • 31P-NMR study on the binding of 3′-cytidine monophosphate to ribonuclease A. I
    • 31P-NMR study on the binding of 3′-cytidine monophosphate to ribonuclease A. I. Biochem. Biophys. Res. Commun. 54:976-982.
    • (1973) Biochem. Biophys. Res. Commun. , vol.54 , pp. 976-982
    • Gorenstein, D.G.1    Wyrwicz, A.2
  • 27
    • 0015919554 scopus 로고
    • Chemical kinetic and proton magnetic resonance studies of 5′-adenosine monophosphate binding to ribonuclease A
    • Haffner, P. H., and J. H. Wang. 1973. Chemical kinetic and proton magnetic resonance studies of 5′-adenosine monophosphate binding to ribonuclease A. Biochemistry. 12:1608-1618.
    • (1973) Biochemistry , vol.12 , pp. 1608-1618
    • Haffner, P.H.1    Wang, J.H.2
  • 28
    • 0021396489 scopus 로고
    • Some evidence suggesting the existence of P2 and B3 sites in the active site of bovine pancreatic ribonuclease A
    • Irie, M., H. Watanabe, K. Ohgi, M. Tobe, G. Matsumura, Y. Arata, T. Hirose, and S. Inayama. 1984. Some evidence suggesting the existence of P2 and B3 sites in the active site of bovine pancreatic ribonuclease A. J. Biochem. 95:751-759.
    • (1984) J. Biochem. , vol.95 , pp. 751-759
    • Irie, M.1    Watanabe, H.2    Ohgi, K.3    Tobe, M.4    Matsumura, G.5    Arata, Y.6    Hirose, T.7    Inayama, S.8
  • 30
    • 0000032631 scopus 로고
    • Topochemical principles of the substrate specificity of nucleases
    • Karpeisky, M. Y., and G. I. Yakovlev. 1981. Topochemical principles of the substrate specificity of nucleases. Sov. Sci. Rev., Sect. D. 2:145-257.
    • (1981) Sov. Sci. Rev., Sect. D. , vol.2 , pp. 145-257
    • Karpeisky, M.Y.1    Yakovlev, G.I.2
  • 31
    • 0014192404 scopus 로고
    • Tertiary structure of ribonuclease
    • Kartha, G., J. Bello, and D. Harker. 1967. Tertiary structure of ribonuclease. Nature. 213:862-865.
    • (1967) Nature , vol.213 , pp. 862-865
    • Kartha, G.1    Bello, J.2    Harker, D.3
  • 32
    • 0018508676 scopus 로고
    • The aromatic residues of bovine pancreatic ribonuclease studied by proton nuclear magnetic resonance
    • Lenstra, J. A., B. G. J. M. Bolscher, S. Stob, J. J. Beintema, and R. Kaptein. 1979. The aromatic residues of bovine pancreatic ribonuclease studied by proton nuclear magnetic resonance. Eur. J. Biochem. 98:385-397.
    • (1979) Eur. J. Biochem. , vol.98 , pp. 385-397
    • Lenstra, J.A.1    Bolscher, B.G.J.M.2    Stob, S.3    Beintema, J.J.4    Kaptein, R.5
  • 33
    • 0016743108 scopus 로고
    • Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. II. The pH and inhibitor-induced conformational transitions affecting histidine-48 and one tyrosine residue of ribonuclease A
    • Markley, J. L. 1975a. Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. II. The pH and inhibitor-induced conformational transitions affecting histidine-48 and one tyrosine residue of ribonuclease A. Biochemistry. 14:3554-3561.
    • (1975) Biochemistry , vol.14 , pp. 3554-3561
    • Markley, J.L.1
  • 34
    • 0016712783 scopus 로고
    • Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignment
    • Markley, J. L. 1975b. Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignment. Biochemistry. 14:3546-3553.
    • (1975) Biochemistry , vol.14 , pp. 3546-3553
    • Markley, J.L.1
  • 35
    • 0016754174 scopus 로고
    • Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. III. Mutual electrostatic interaction between histidine residues 12 and 119
    • Markley, J. L., and W. R. Finkenstadt. 1975. Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. III. Mutual electrostatic interaction between histidine residues 12 and 119. Biochemistry. 14:3562-3566.
    • (1975) Biochemistry , vol.14 , pp. 3562-3566
    • Markley, J.L.1    Finkenstadt, W.R.2
  • 36
    • 0022515682 scopus 로고
    • The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease
    • McPherson, A., G. Brayer, D. Cascio, and R. Williams. 1986. The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease. Science. 232:765-768.
    • (1986) Science , vol.232 , pp. 765-768
    • McPherson, A.1    Brayer, G.2    Cascio, D.3    Williams, R.4
  • 37
    • 0032476051 scopus 로고    scopus 로고
    • The subsites structure of bovine pancreatic ribonuclease A account for the abnormal kinetic behavior with cytidine 2′,3′-cyclic phosphate
    • Moussaoui, M., M. V. Nogués, A. Guasch, T. Barman, F. Travers, and C. M. Cuchillo. 1998. The subsites structure of bovine pancreatic ribonuclease A account for the abnormal kinetic behavior with cytidine 2′,3′-cyclic phosphate. J. Biol. Chem. 273:25562-25572.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25562-25572
    • Moussaoui, M.1    Nogués, M.V.2    Guasch, A.3    Barman, T.4    Travers, F.5    Cuchillo, C.M.6
  • 38
    • 0028806062 scopus 로고
    • Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites
    • Nogués, M. V., M. Vilanova, and C. M. Cuchillo. 1995. Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites. Biochim. Biophys. Acta. 1253:16-24.
    • (1995) Biochim. Biophys. Acta. , vol.1253 , pp. 16-24
    • Nogués, M.V.1    Vilanova, M.2    Cuchillo, C.M.3
  • 41
    • 0032558938 scopus 로고    scopus 로고
    • His ⋯ Asp catalytic dyad of ribonuclease A: Conformational stability of the wild-type, D121N, D121A, and H119A enzymes
    • Quirk, D. J., C. Park, J. E. Thompson, and R. T. Raines. 1998. His ⋯ Asp catalytic dyad of ribonuclease A: conformational stability of the wild-type, D121N, D121A, and H119A enzymes. Biochemistry. 37: 17958-17964.
    • (1998) Biochemistry , vol.37 , pp. 17958-17964
    • Quirk, D.J.1    Park, C.2    Thompson, J.E.3    Raines, R.T.4
  • 42
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines, R. T. 1998. Ribonuclease A. Chem. Rev. 98:1045-1065.
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 44
    • 0024384662 scopus 로고
    • Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution
    • Robertson, A. D., E. O. Purisima, M. A. Eastman, and H. A. Scheraga. 1989. Proton NMR assignments and regular backbone structure of bovine pancreatic ribonuclease A in aqueous solution. Biochemistry. 1989:5930-5938.
    • (1989) Biochemistry , vol.1989 , pp. 5930-5938
    • Robertson, A.D.1    Purisima, E.O.2    Eastman, M.A.3    Scheraga, H.A.4
  • 45
    • 0000433758 scopus 로고
    • The nuclear magnetic resonance spectrum of ribonuclease
    • Saunders, M., A. Wishnia, and J. Kirkwood. 1957. The nuclear magnetic resonance spectrum of ribonuclease. J. Am. Chem. Soc. 79:3289.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 3289
    • Saunders, M.1    Wishnia, A.2    Kirkwood, J.3
  • 46
    • 0032560446 scopus 로고    scopus 로고
    • His ⋯ Asp catalytic dyad of ribonuclease A: Structure and function of the wild-type, D121N, and D121A enzymes
    • Schultz, L. W., D. J. Quirk, and R. T. Raines. 1998. His ⋯ Asp catalytic dyad of ribonuclease A: structure and function of the wild-type, D121N, and D121A enzymes. Biochemistry. 37:8886-8898.
    • (1998) Biochemistry , vol.37 , pp. 8886-8898
    • Schultz, L.W.1    Quirk, D.J.2    Raines, R.T.3
  • 47
    • 0000231043 scopus 로고
    • The correlation of ribonuclease activity with specific aspects of tertiary structure
    • Sela, M., C. B. Anfinsen, and W. F. Harrington. 1957. The correlation of ribonuclease activity with specific aspects of tertiary structure. Biochim. Biophys. Acta. 26:502-512.
    • (1957) Biochim. Biophys. Acta. , vol.26 , pp. 502-512
    • Sela, M.1    Anfinsen, C.B.2    Harrington, W.F.3
  • 48
    • 0015507243 scopus 로고
    • Mathematical models for interacting groups in nuclear magnetic resonance titration curves
    • Shrager, R. I., J. S. Cohen, S. R. Heller, D. H. Sachs, and A. N. Schechter. 1972. Mathematical models for interacting groups in nuclear magnetic resonance titration curves. Biochemistry. 11:541-547.
    • (1972) Biochemistry , vol.11 , pp. 541-547
    • Shrager, R.I.1    Cohen, J.S.2    Heller, S.R.3    Sachs, D.H.4    Schechter, A.N.5
  • 49
    • 0000831938 scopus 로고
    • The sequence of amino acid residues in bovine pancreatic ribonuclease: Revisions and confirmations
    • Smythe, D. G., W. H. Stein, and S. Moore. 1963. The sequence of amino acid residues in bovine pancreatic ribonuclease: revisions and confirmations. J. Biol. Chem. 238:227.
    • (1963) J. Biol. Chem. , vol.238 , pp. 227
    • Smythe, D.G.1    Stein, W.H.2    Moore, S.3
  • 50
    • 0021103502 scopus 로고
    • Proton NMR study on the tautomerism of the imidazole ring of histidine residues. II. Microenvironments of histidine-12 and histidine-119 of bovine pancreatic ribonuclease A
    • Tanokura, M. 1983. Proton NMR study on the tautomerism of the imidazole ring of histidine residues. II. Microenvironments of histidine-12 and histidine-119 of bovine pancreatic ribonuclease A. Biochim. Biophys. Acta. 742:586-596.
    • (1983) Biochim. Biophys. Acta. , vol.742 , pp. 586-596
    • Tanokura, M.1
  • 51
    • 0027949817 scopus 로고
    • Value of general acid-base catalysis to ribonuclease A
    • Thompson, J. E., and R. T. Raines. 1994. Value of general acid-base catalysis to ribonuclease A. J. Am. Chem. Soc. 116:5467-5468.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 5467-5468
    • Thompson, J.E.1    Raines, R.T.2
  • 52
    • 0028364742 scopus 로고
    • Energetics of catalysis by ribonucleases: Fate of the 2′,3′-cyclic intermediate
    • Thompson, J. E., F. D. Venegas, and R. T. Raines. 1994. Energetics of catalysis by ribonucleases: fate of the 2′,3′-cyclic intermediate. Biochemistry. 33:7408-7414.
    • (1994) Biochemistry , vol.33 , pp. 7408-7414
    • Thompson, J.E.1    Venegas, F.D.2    Raines, R.T.3
  • 53
    • 0023758305 scopus 로고
    • NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A
    • Udgaonkar, J., and R. Baldwin. 1988. NMR evidence for an early framework intermediate on the folding pathway of ribonuclease A. Science. 335:694-699.
    • (1988) Science , vol.335 , pp. 694-699
    • Udgaonkar, J.1    Baldwin, R.2
  • 54
    • 0141813820 scopus 로고
    • Spectrophotometric study of the hydrolysis constants of the negative ions of some aryl imidazoles
    • Walba, H., and R. W. Isensee. 1955. Spectrophotometric study of the hydrolysis constants of the negative ions of some aryl imidazoles. J. Am. Chem. Soc. 77:5488-5492.
    • (1955) J. Am. Chem. Soc. , vol.77 , pp. 5488-5492
    • Walba, H.1    Isensee, R.W.2
  • 56
    • 0032503565 scopus 로고    scopus 로고
    • Structure (1.3 Å) and charge states of a ribonuclease A-uridine vanadate complex: Implications for the phosphate ester hydrolysis mechanism
    • Wladkowski, B. D., L. A. Svensson, L. Sjolin, J. E. Ladner, and G. L. Gilliland. 1998. Structure (1.3 Å) and charge states of a ribonuclease A-uridine vanadate complex: implications for the phosphate ester hydrolysis mechanism. J. Am. Chem. Soc. 120:5488-5498.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 5488-5498
    • Wladkowski, B.D.1    Svensson, L.A.2    Sjolin, L.3    Ladner, J.E.4    Gilliland, G.L.5
  • 57
    • 0020772531 scopus 로고
    • Active site of RNase: Neutron diffraction study of a complex with undine vanadate, a transition-state analog
    • Wlodawer, A., M. Miller, and L. Sjölin. 1983. Active site of RNase: neutron diffraction study of a complex with undine vanadate, a transition-state analog. Proc. Natl. Acad. Sci. U.S.A. 80:3628-3631.
    • (1983) Proc. Natl. Acad. Sci. U.S.A , vol.80 , pp. 3628-3631
    • Wlodawer, A.1    Miller, M.2    Sjölin, L.3
  • 58
    • 0003620527 scopus 로고
    • University Science Books, Mill Valley, CA
    • Wyman, J., and S. J. Gill. 1990. Binding and Linkage. University Science Books, Mill Valley, CA.
    • (1990) Binding and Linkage
    • Wyman, J.1    Gill, S.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.