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Volumn 2, Issue 1, 1997, Pages 53-66

All in one: A highly detailed rotamer library improves both accuracy and speed in the modelling of sidechains by dead-end elimination

Author keywords

Dead end elimination; Global energy minimum; Homology modelling; Rotamer library; Rotamers

Indexed keywords

ALGORITHM; ARTICLE; AUDIOVISUAL EQUIPMENT; CHEMICAL MODEL; PROTEIN CONFORMATION; PROTEIN FOLDING;

EID: 0030623575     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/s1359-0278(97)00006-0     Document Type: Article
Times cited : (116)

References (65)
  • 1
    • 0018115846 scopus 로고
    • Conformation of amino acid side-chains in proteins
    • Janin, J., Wodak, S., Levitt, M. & Maigret, B. (1978). Conformation of amino acid side-chains in proteins. J. Mol. Biol. 125, 357-386.
    • (1978) J. Mol. Biol. , vol.125 , pp. 357-386
    • Janin, J.1    Wodak, S.2    Levitt, M.3    Maigret, B.4
  • 3
    • 0020685129 scopus 로고
    • Structure and refinement of penicillopepsin at 1.8 Å resolution
    • James, M.N.G. & Sielecki, A.R. (1983). Structure and refinement of penicillopepsin at 1.8 Å resolution. J. Mol. Biol. 163, 299-361.
    • (1983) J. Mol. Biol. , vol.163 , pp. 299-361
    • James, M.N.G.1    Sielecki, A.R.2
  • 4
  • 5
    • 0023155210 scopus 로고
    • Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes
    • Ponder, J.W. & Richards, P.M. (1987). Tertiary templates for proteins. Use of packing criteria in the enumeration of allowed sequences for different structural classes. J. Mol. Biol. 193, 775-791.
    • (1987) J. Mol. Biol. , vol.193 , pp. 775-791
    • Ponder, J.W.1    Richards, P.M.2
  • 6
    • 0023645193 scopus 로고
    • An analysis of side-chain orientations in homologous proteins
    • Summers, N.L, Carson, W.D. & Karplus. M. (1987). An analysis of side-chain orientations in homologous proteins. J. Mol. Biol. 196, 157-198.
    • (1987) J. Mol. Biol. , vol.196 , pp. 157-198
    • Summers, N.L.1    Carson, W.D.2    Karplus, M.3
  • 7
    • 0023521842 scopus 로고
    • Analysis of the relationship between side-chain conformation and secondary structure in globular proteins
    • McGregor, M.J., Islam, S.A. & Sternberg, M.J.E. (1987). Analysis of the relationship between side-chain conformation and secondary structure in globular proteins. J. Mol. Biol. 198, 295-310.
    • (1987) J. Mol. Biol. , vol.198 , pp. 295-310
    • McGregor, M.J.1    Islam, S.A.2    Sternberg, M.J.E.3
  • 8
    • 0028991962 scopus 로고
    • Modelling mutations and homologous proteins
    • Šali, A. (1995). Modelling mutations and homologous proteins. Curr. Opin. Biotechnol. 6, 437-451.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 437-451
    • Šali, A.1
  • 9
    • 0141560472 scopus 로고    scopus 로고
    • Modeling side-chain conformation
    • Vásquez, M. (1996). Modeling side-chain conformation. Curr. Opin. Struct. Biol. 6, 217-221.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 217-221
    • Vásquez, M.1
  • 10
    • 0025978283 scopus 로고
    • Database algorithm for generating protein backbone and side-chain co-ordinates from a Cα trace: Application to model building and detection of co-ordinate errors
    • Holm, L. & Sander, C. (1991). Database algorithm for generating protein backbone and side-chain co-ordinates from a Cα trace: application to model building and detection of co-ordinate errors. J. Mol. Biol. 218, 183-194.
    • (1991) J. Mol. Biol. , vol.218 , pp. 183-194
    • Holm, L.1    Sander, C.2
  • 11
    • 0026675799 scopus 로고
    • Fast and simple Monte Carlo algorithm for side-chain optimization in proteins: Application to model building by homology
    • Holm, L. & Sander, C. (1992). Fast and simple Monte Carlo algorithm for side-chain optimization in proteins: application to model building by homology. Proteins 14, 213-223.
    • (1992) Proteins , vol.14 , pp. 213-223
    • Holm, L.1    Sander, C.2
  • 12
    • 0028223845 scopus 로고
    • Predicting protein mutant energetics by selfconsistent ensemble optimization
    • Lee, C. (1994). Predicting protein mutant energetics by selfconsistent ensemble optimization. J. Mol. Biol. 236, 918-939.
    • (1994) J. Mol. Biol. , vol.236 , pp. 918-939
    • Lee, C.1
  • 13
    • 0026179489 scopus 로고
    • A new approach to the rapid determination of protein side chain conformations
    • Tufféry, P., Etchebest, C., Hazout, S. & Lavery, R. (1991). A new approach to the rapid determination of protein side chain conformations. J. Biomol. Struct. Dynam. 8, 1267-1289.
    • (1991) J. Biomol. Struct. Dynam. , vol.8 , pp. 1267-1289
    • Tufféry, P.1    Etchebest, C.2    Hazout, S.3    Lavery, R.4
  • 14
    • 84913539119 scopus 로고
    • A critical comparison of search algorithm applied to the optimization of protein side-chain conformations
    • Tufféry, P., Etchebest, C., Hazout, S. & Lavery, R. (1993). A critical comparison of search algorithm applied to the optimization of protein side-chain conformations. J. Comput. Chem. 14, 790-798.
    • (1993) J. Comput. Chem. , vol.14 , pp. 790-798
    • Tufféry, P.1    Etchebest, C.2    Hazout, S.3    Lavery, R.4
  • 15
    • 0027480460 scopus 로고
    • Modeling side-chain conformation for homologous proteins using an energy-based rotamer search
    • Wilson, C., Gregoret, L.M. & Agard, D.A. (1993). Modeling side-chain conformation for homologous proteins using an energy-based rotamer search. J. Mol. Biol. 229, 996-1006.
    • (1993) J. Mol. Biol. , vol.229 , pp. 996-1006
    • Wilson, C.1    Gregoret, L.M.2    Agard, D.A.3
  • 16
    • 0025288651 scopus 로고
    • The building of protein structures from alpha-carbon coordinates
    • Correa, P.E. (1990). The building of protein structures from alpha-carbon coordinates. Proteins 7, 366-377.
    • (1990) Proteins , vol.7 , pp. 366-377
    • Correa, P.E.1
  • 17
    • 0026019108 scopus 로고
    • Prediction of protein sidechain conformation by packing optimization
    • Lee, C. & Subbiah, S. (1991). Prediction of protein sidechain conformation by packing optimization. J. Mol. Biol. 217, 373-388.
    • (1991) J. Mol. Biol. , vol.217 , pp. 373-388
    • Lee, C.1    Subbiah, S.2
  • 18
    • 0025280307 scopus 로고
    • Prediction of homologous protein structures based on conformational searches and energetics
    • Schiffer, C.A, Caldwell, J.W., Kollman, P.A. & Stroud, R.M. (1990). Prediction of homologous protein structures based on conformational searches and energetics. Proteins 8, 30-43.
    • (1990) Proteins , vol.8 , pp. 30-43
    • Schiffer, C.A.1    Caldwell, J.W.2    Kollman, P.A.3    Stroud, R.M.4
  • 19
    • 0027185404 scopus 로고
    • A method to configure protein side-chains from the main-chain trace in homology modelling
    • Eisenmenger, F., Argos, P. & Abagyan, R. (1993). A method to configure protein side-chains from the main-chain trace in homology modelling. J. Mol. Biol. 231, 849-860.
    • (1993) J. Mol. Biol. , vol.231 , pp. 849-860
    • Eisenmenger, F.1    Argos, P.2    Abagyan, R.3
  • 20
    • 0028140474 scopus 로고
    • Prediction of protein side-chain conformations from local three-dimensional homology relationships
    • Laughton, C.A. (1994). Prediction of protein side-chain conformations from local three-dimensional homology relationships. J. Mol. Biol. 235, 1088-1097.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1088-1097
    • Laughton, C.A.1
  • 21
    • 0028304155 scopus 로고
    • Energy minimization method using automata network for sequence and side-chain conformation prediction from given backbone geometry
    • Kono, H. & Doi, J. (1994). Energy minimization method using automata network for sequence and side-chain conformation prediction from given backbone geometry. Proteins 19, 244-255.
    • (1994) Proteins , vol.19 , pp. 244-255
    • Kono, H.1    Doi, J.2
  • 22
    • 0028343413 scopus 로고
    • Application of a selfconsistent mean field theory to predict protein side-chains conformation and estimate their conformational entropy
    • Koehl, P. & Delarue, M. (1994). Application of a selfconsistent mean field theory to predict protein side-chains conformation and estimate their conformational entropy. J. Mol. Biol. 239, 249-275.
    • (1994) J. Mol. Biol. , vol.239 , pp. 249-275
    • Koehl, P.1    Delarue, M.2
  • 23
    • 0026754015 scopus 로고
    • Accurate modelling of protein conformation by automatic segment matching
    • Levitt, M. (1992). Accurate modelling of protein conformation by automatic segment matching. J. Mol. Biol. 226, 507-533.
    • (1992) J. Mol. Biol. , vol.226 , pp. 507-533
    • Levitt, M.1
  • 24
    • 0026589733 scopus 로고
    • The dead-end elimination theorem and its use in protein sidechain positioning
    • Desmet, J., De Maeyer, M., Hazes, B. & Lasters, I. (1992). The dead-end elimination theorem and its use in protein sidechain positioning. Nature 356, 539-542.
    • (1992) Nature , vol.356 , pp. 539-542
    • Desmet, J.1    De Maeyer, M.2    Hazes, B.3    Lasters, I.4
  • 25
    • 0027493639 scopus 로고
    • The fuzzy-end elimination theorem: Correctly implementing the side-chain placement algorithm based on the dead-end elimination theorem
    • Lasters, I. & Desmet, J. (1993). The fuzzy-end elimination theorem: correctly implementing the side-chain placement algorithm based on the dead-end elimination theorem. Protein Eng. 6, 717-722.
    • (1993) Protein Eng. , vol.6 , pp. 717-722
    • Lasters, I.1    Desmet, J.2
  • 26
    • 0028212927 scopus 로고
    • Efficient rotamer elimination applied to protein side-chains and related spin glasses
    • Goldstein, R.F. (1994). Efficient rotamer elimination applied to protein side-chains and related spin glasses. Biophys. J. 66, 1335-1340.
    • (1994) Biophys. J. , vol.66 , pp. 1335-1340
    • Goldstein, R.F.1
  • 27
    • 0028598623 scopus 로고
    • Determinants of protein side-chain packing
    • Tanimura, R., Kidera, A. & Nakamura, H. (1994). Determinants of protein side-chain packing. Protein Sci. 3, 2358-2365.
    • (1994) Protein Sci. , vol.3 , pp. 2358-2365
    • Tanimura, R.1    Kidera, A.2    Nakamura, H.3
  • 28
    • 0029591934 scopus 로고
    • Finding the global minimum: A fuzzy end elimination implementation
    • Keller, K.A., Shibata, M., Marcus, E., Ornstein, R.L. & Rein, R. (1995). Finding the global minimum: a fuzzy end elimination implementation. Protein Eng. 8, 893-904.
    • (1995) Protein Eng. , vol.8 , pp. 893-904
    • Keller, K.A.1    Shibata, M.2    Marcus, E.3    Ornstein, R.L.4    Rein, R.5
  • 29
    • 0028826985 scopus 로고
    • Enhanced dead-end elimination in the search for the global minimum energy conformation of a collection of protein side-chains
    • Lasters, I., De Maeyer, M. & Desmet, J. (1995). Enhanced dead-end elimination in the search for the global minimum energy conformation of a collection of protein side-chains. Protein Eng. 8, 815-822.
    • (1995) Protein Eng. , vol.8 , pp. 815-822
    • Lasters, I.1    De Maeyer, M.2    Desmet, J.3
  • 30
    • 0029920337 scopus 로고    scopus 로고
    • Protein design automation
    • Dahiyat, B.L. & Mayo, S.L. (1996). Protein design automation. Protein Sci. 5, 895-903.
    • (1996) Protein Sci. , vol.5 , pp. 895-903
    • Dahiyat, B.L.1    Mayo, S.L.2
  • 32
    • 0027208112 scopus 로고
    • Rotamers: To be or not to be? An analysis of amino acid side-chain conformations in globular proteins
    • Schrauber, H., Eisenhaber, F. & Argos, P. (1993). Rotamers: to be or not to be? An analysis of amino acid side-chain conformations in globular proteins. J. Mol. Biol. 230, 592-612.
    • (1993) J. Mol. Biol. , vol.230 , pp. 592-612
    • Schrauber, H.1    Eisenhaber, F.2    Argos, P.3
  • 33
    • 0023645203 scopus 로고
    • Interior and surface of monomeric proteins
    • Miller, S., Janin, J., Lesk, A.M. & Chothia, C. (1987). Interior and surface of monomeric proteins. J. Mol. Biol. 196, 641-656.
    • (1987) J. Mol. Biol. , vol.196 , pp. 641-656
    • Miller, S.1    Janin, J.2    Lesk, A.M.3    Chothia, C.4
  • 34
    • 0029058162 scopus 로고
    • Side-chain prediction by neural networks and simulated annealing optimization
    • Hwang, J. & Liao, W. (1995). Side-chain prediction by neural networks and simulated annealing optimization. Protein Eng. 8, 363-370.
    • (1995) Protein Eng. , vol.8 , pp. 363-370
    • Hwang, J.1    Liao, W.2
  • 35
    • 0027160197 scopus 로고
    • Backbone-dependent rotamer library for proteins: Application to side-chain prediction
    • Dunbrack, R.L., Jr. & Karplus, M. (1993). Backbone-dependent rotamer library for proteins: application to side-chain prediction. J. Mol. Biol. 230, 543-574.
    • (1993) J. Mol. Biol. , vol.230 , pp. 543-574
    • Dunbrack Jr., R.L.1    Karplus, M.2
  • 36
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjelgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjelgaard, M.4
  • 37
    • 0028154121 scopus 로고
    • Crystal structure of RNase T1 with 3′-guanylic acid and guanosine
    • Zegers, I., Haikal, A.F., Palmer, R. & Wyns, L (1994). Crystal structure of RNase T1 with 3′-guanylic acid and guanosine. J. Biol. Chem. 269, 127-133.
    • (1994) J. Biol. Chem. , vol.269 , pp. 127-133
    • Zegers, I.1    Haikal, A.F.2    Palmer, R.3    Wyns, L.4
  • 38
    • 0027934929 scopus 로고
    • Automated comparative modelling of protein structures
    • May, A.C.W. & Blundell, T.L. (1994). Automated comparative modelling of protein structures. Curr. Opin. Biotechnol. 5, 355-360.
    • (1994) Curr. Opin. Biotechnol. , vol.5 , pp. 355-360
    • May, A.C.W.1    Blundell, T.L.2
  • 39
    • 0023645795 scopus 로고
    • Structure determination of the glucosomal triosphosphate isomerase from Trypanosoma brucei brucei at 2.4 Å resolution
    • Wierenga, R.K., Kalk, K.H. & Hol, W.G.J. (1987). Structure determination of the glucosomal triosphosphate isomerase from Trypanosoma brucei brucei at 2.4 Å resolution. J. Mol. Biol. 198, 109-121.
    • (1987) J. Mol. Biol. , vol.198 , pp. 109-121
    • Wierenga, R.K.1    Kalk, K.H.2    Hol, W.G.J.3
  • 40
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of a helices
    • Richardson, J.S. & Richardson, D.C. (1988). Amino acid preferences for specific locations at the ends of a helices. Science 240, 1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 41
    • 0014966180 scopus 로고
    • Abbreviations and symbols for the description of the conformation of polypeptide chains
    • IUPAC-IUB Commission on Biochemical Nomenclature. (1970). Abbreviations and symbols for the description of the conformation of polypeptide chains. J. Mol. Biol. 52, 1-17.
    • (1970) J. Mol. Biol. , vol.52 , pp. 1-17
  • 42
    • 0022844865 scopus 로고
    • Modification of human hemoglobin by gluthadione. III Perturbations of hemoglobin conformation analyzed by computer modeling
    • Wodak, S., De Coen, J.L., Edelstein, S.J., Demarne, H. & Beuzard, Y. (1986). Modification of human hemoglobin by gluthadione. III Perturbations of hemoglobin conformation analyzed by computer modeling. J. Biol. Chem. 261, 14717-14724.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14717-14724
    • Wodak, S.1    De Coen, J.L.2    Edelstein, S.J.3    Demarne, H.4    Beuzard, Y.5
  • 43
    • 0017411710 scopus 로고
    • The Protein Data Bank: A computer-based archival file for macromolecular structures
    • Bernstein, F.C., et al., & Tasumi, M. (1977). The Protein Data Bank: a computer-based archival file for macromolecular structures. J. Mol. Biol. 112, 535-542.
    • (1977) J. Mol. Biol. , vol.112 , pp. 535-542
    • Bernstein, F.C.1    Tasumi, M.2
  • 44
    • 0024281641 scopus 로고
    • Three-dimensional structure at 0.86 angstroms of the uncomplexed form of the transmembrane channel peptide gramicidin
    • Langs, DA (1988). Three-dimensional structure at 0.86 angstroms of the uncomplexed form of the transmembrane channel peptide gramicidin. Science 241, 188-191.
    • (1988) Science , vol.241 , pp. 188-191
    • Langs, D.A.1
  • 45
    • 0019450355 scopus 로고
    • Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur
    • Hendrickson, W.A., Teeter, M.M. (1981). Structure of the hydrophobic protein crambin determined directly from the anomalous scattering of sulphur. Nature 290, 107-113.
    • (1981) Nature , vol.290 , pp. 107-113
    • Hendrickson, W.A.1    Teeter, M.M.2
  • 46
    • 0002841934 scopus 로고
    • Refinement of rubredoxin from Desulfovibrio vulgaris at 1.0 Å with and without restraints
    • Dauter, Z., Sieker, L.C. & Wilson, K.S. (1992). Refinement of rubredoxin from Desulfovibrio vulgaris at 1.0 Å with and without restraints. Acta. Crystallogr. B 48, 42-59.
    • (1992) Acta. Crystallogr. B , vol.48 , pp. 42-59
    • Dauter, Z.1    Sieker, L.C.2    Wilson, K.S.3
  • 47
    • 0021603710 scopus 로고
    • Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II
    • Wlodawer, A., Walter, J., Huber, R. & Sjolin, L. (1984). Structure of bovine pancreatic trypsin inhibitor. Results of joint neutron and X-ray refinement of crystal form II. J. Mol. Biol. 180, 301-329.
    • (1984) J. Mol. Biol. , vol.180 , pp. 301-329
    • Wlodawer, A.1    Walter, J.2    Huber, R.3    Sjolin, L.4
  • 48
    • 0026646490 scopus 로고
    • Structure of scorpion toxin variant-3 at 1.2 Å resolution
    • Zhao, B., Carson, M., Ealick, S.E. & Bugg, C.E. (1992). Structure of scorpion toxin variant-3 at 1.2 Å resolution. J. Mol. Biol. 227, 239-252.
    • (1992) J. Mol. Biol. , vol.227 , pp. 239-252
    • Zhao, B.1    Carson, M.2    Ealick, S.E.3    Bugg, C.E.4
  • 49
    • 0028080176 scopus 로고
    • The third IgG-binding domain from streptococcal protein G. An analysis by X-ray crystallography of the structure alone and in a complex with Fab
    • Derrick, J.P. & Wigley, D.B. (1994). The third IgG-binding domain from streptococcal protein G. An analysis by X-ray crystallography of the structure alone and in a complex with Fab. J. Mol. Biol. 243, 906-918.
    • (1994) J. Mol. Biol. , vol.243 , pp. 906-918
    • Derrick, J.P.1    Wigley, D.B.2
  • 50
    • 0020004138 scopus 로고
    • Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms
    • Matsuura, Y., Takano, T. & Dickerson, R.E. (1982). Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms. J. Mol. Biol. 156, 389-409.
    • (1982) J. Mol. Biol. , vol.156 , pp. 389-409
    • Matsuura, Y.1    Takano, T.2    Dickerson, R.E.3
  • 52
    • 0019816864 scopus 로고
    • Refinement of human lysozyme at 1.5 Å resolution analysis of non-bonded and hydrogen-bond interactions
    • Artymiuk, P.J. & Blake, C.C. (1981). Refinement of human lysozyme at 1.5 Å resolution analysis of non-bonded and hydrogen-bond interactions. J. Mol. Biol. 152, 737-762.
    • (1981) J. Mol. Biol. , vol.152 , pp. 737-762
    • Artymiuk, P.J.1    Blake, C.C.2
  • 53
    • 0028564999 scopus 로고
    • The structures of RNase a complexed with 3′-CMP and d(CpA): Active site conformation and conserved water molecules
    • Zegers, I., Maes, D., Dao-Thi, M.H., Poortmans, F., Palmer, R. & Wyns, L. (1994). The structures of RNase A complexed with 3′-CMP and d(CpA): active site conformation and conserved water molecules. Protein Sci. 3, 2322-2339.
    • (1994) Protein Sci. , vol.3 , pp. 2322-2339
    • Zegers, I.1    Maes, D.2    Dao-Thi, M.H.3    Poortmans, F.4    Palmer, R.5    Wyns, L.6
  • 54
    • 0024293340 scopus 로고
    • Structure of azurin from Alcaligenes denitrificans refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules
    • Baker, E.N. (1988). Structure of azurin from Alcaligenes denitrificans refinement at 1.8 Å resolution and comparison of the two crystallographically independent molecules. J. Mol. Biol. 203, 1071-1095.
    • (1988) J. Mol. Biol. , vol.203 , pp. 1071-1095
    • Baker, E.N.1
  • 55
    • 0024961706 scopus 로고
    • Aplysia limacina myoglobin. Crystallographic analysis at 1.6 Å resolution
    • Bolognesi, M., Onesti, S., Gatti, G., Coda, A., Ascenzi, P. & Brunori, M. (1989). Aplysia limacina myoglobin. Crystallographic analysis at 1.6 Å resolution. J. Mol. Biol. 205, 529-544.
    • (1989) J. Mol. Biol. , vol.205 , pp. 529-544
    • Bolognesi, M.1    Onesti, S.2    Gatti, G.3    Coda, A.4    Ascenzi, P.5    Brunori, M.6
  • 56
    • 0027096161 scopus 로고
    • Refinement of the structure of Escherichia cofrderived rat intestinal fatty acid binding protein with bound oleate to 1.75-Å resolution. Correlation with the structures of the apoprotein and the protein with bound palmitate
    • Sacchettini, J.C., Scapin, G., Gopaul, D. & Gordon, J.I. (1992). Refinement of the structure of Escherichia cofrderived rat intestinal fatty acid binding protein with bound oleate to 1.75-Å resolution. Correlation with the structures of the apoprotein and the protein with bound palmitate. J. Biol. Chem. 267, 23534-23545.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23534-23545
    • Sacchettini, J.C.1    Scapin, G.2    Gopaul, D.3    Gordon, J.I.4
  • 57
    • 0024961747 scopus 로고
    • The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease
    • Tsunasawa, S., Masaki, T., Hirose, M., Soejima, M. & Sakiyama, F. (1989). The primary structure and structural characteristics of Achromobacter lyticus protease I, a lysine-specific serine protease. J. Biol. Chem. 264, 3832-3839.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3832-3839
    • Tsunasawa, S.1    Masaki, T.2    Hirose, M.3    Soejima, M.4    Sakiyama, F.5
  • 58
    • 0016291686 scopus 로고
    • Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution
    • Huber, R., et al., & Steigemann, W.S.O. (1974). Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 Å resolution. J. Mol. Biol. 89, 73-101.
    • (1974) J. Mol. Biol. , vol.89 , pp. 73-101
    • Huber, R.1    Steigemann, W.S.O.2
  • 59
    • 0023643147 scopus 로고
    • The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry
    • Bode, W., Papamokos, E. & Musil, D. (1987). The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry. Eur. J. Biochem. 166, 673-692.
    • (1987) Eur. J. Biochem. , vol.166 , pp. 673-692
    • Bode, W.1    Papamokos, E.2    Musil, D.3
  • 60
    • 0020462668 scopus 로고
    • Structure of thermolysin refined at 1.6 Å resolution. 7
    • Holmes, M.A. & Matthews, B.W. (1982). Structure of thermolysin refined at 1.6 Å resolution. 7. Mol. Biol. 160, 623-639.
    • (1982) Mol. Biol. , vol.160 , pp. 623-639
    • Holmes, M.A.1    Matthews, B.W.2
  • 62
    • 0001588881 scopus 로고
    • Detection of cavities in a set of interpenetrating spheres
    • Alard, P. & Wodak, S.J. (1991). Detection of cavities in a set of interpenetrating spheres. J. Comp. Chem. 12, 918-922.
    • (1991) J. Comp. Chem. , vol.12 , pp. 918-922
    • Alard, P.1    Wodak, S.J.2
  • 63
    • 0002426606 scopus 로고
    • Interactive computer animation of macromolecules
    • Delhaise, P., Bardiaux, M. & Wodak, S. (1984). Interactive computer animation of macromolecules. J. Mol. Graph. 2, 103-106.
    • (1984) J. Mol. Graph. , vol.2 , pp. 103-106
    • Delhaise, P.1    Bardiaux, M.2    Wodak, S.3
  • 64
    • 0017100947 scopus 로고
    • Theoretical studies of enzymatic reactions: Dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme
    • Warshel, A. & Levitt, M. (1976). Theoretical studies of enzymatic reactions: dielectric, electrostatic and steric stabilization of the carbonium ion in the reaction of lysozyme. J. Mol. Biol. 103, 227-249.
    • (1976) J. Mol. Biol. , vol.103 , pp. 227-249
    • Warshel, A.1    Levitt, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.