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Volumn 32, Issue 2, 1998, Pages 159-174

Flexible docking allowing induced fit in proteins: Insights from an open to closed conformational isomers

Author keywords

Flexible docking; Induced fit; Molecular recognition; Protein ligand interaction; Structure based drug design

Indexed keywords

ALGORITHM; ARTICLE; ISOMERISM; LIGAND BINDING; MOLECULAR MODEL; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN CONFORMATION; RECEPTOR BINDING;

EID: 0032147007     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(19980801)32:2<159::AID-PROT3>3.0.CO;2-G     Document Type: Article
Times cited : (106)

References (66)
  • 1
    • 0025708676 scopus 로고
    • Hinge-bending and folding
    • Dobson, C.M. Hinge-bending and folding. Nature 348:198-199, 1990.
    • (1990) Nature , vol.348 , pp. 198-199
    • Dobson, C.M.1
  • 2
    • 0025047629 scopus 로고
    • 4 lysozyme displays five different crystal conformations
    • 4 lysozyme displays five different crystal conformations. Nature 348:263-266, 1990.
    • (1990) Nature , vol.348 , pp. 263-266
    • Faber, H.R.1    Matthews, B.W.2
  • 3
    • 0023661228 scopus 로고
    • Structure of a complex of catabolic gene activator protein and cyclic AMP refined at 2.5Å resolution
    • Weber, I.T., Steitz, T.A. Structure of a complex of catabolic gene activator protein and cyclic AMP refined at 2.5Å resolution. J. Mol. Biol. 198:311-326, 1987.
    • (1987) J. Mol. Biol. , vol.198 , pp. 311-326
    • Weber, I.T.1    Steitz, T.A.2
  • 4
    • 0025015392 scopus 로고
    • Anatomy of conformational change: Hinged "lid" motion of the trisephosphate isomerase loop
    • Joseph, D., Petsko, G.A., Karplus, M. Anatomy of conformational change: Hinged "lid" motion of the trisephosphate isomerase loop. Science, 249:1425-1428, 1990.
    • (1990) Science , vol.249 , pp. 1425-1428
    • Joseph, D.1    Petsko, G.A.2    Karplus, M.3
  • 6
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini, J.M., Schulze-Gahmen, U., Wilson, I.A. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science, 255:959-965, 1992.
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 7
    • 0025321903 scopus 로고
    • Crystal structure of an antibody to a peptide and its complex with peptide antigen at 2.8Å
    • Stanfield, R.L., Fieser, T.M., Lerner, R.A., Wilson, I.A. Crystal structure of an antibody to a peptide and its complex with peptide antigen at 2.8Å. Science, 248:712-719, 1990.
    • (1990) Science , vol.248 , pp. 712-719
    • Stanfield, R.L.1    Fieser, T.M.2    Lerner, R.A.3    Wilson, I.A.4
  • 8
    • 0030821164 scopus 로고    scopus 로고
    • Structural insights into the evolution of an antibody combining site
    • Wedemayer, G.E., Patten, P.A., Wang, L.E., Schultz, P.G., Stevens, R.C. Structural insights into the evolution of an antibody combining site. Science, 276:1665-1669, 1997.
    • (1997) Science , vol.276 , pp. 1665-1669
    • Wedemayer, G.E.1    Patten, P.A.2    Wang, L.E.3    Schultz, P.G.4    Stevens, R.C.5
  • 9
    • 0020655246 scopus 로고
    • Structural domains in proteins and their role in the dynamics of protein function
    • Janin, J., Wodak, S.J. Structural domains in proteins and their role in the dynamics of protein function. Prog. Biophys. Mol. Biol. 42:21-78, 1983.
    • (1983) Prog. Biophys. Mol. Biol. , vol.42 , pp. 21-78
    • Janin, J.1    Wodak, S.J.2
  • 10
    • 0021314461 scopus 로고
    • Structural and functional aspects of domain motion in proteins
    • Bennett, W.S., Huber, R. Structural and functional aspects of domain motion in proteins. CRC Crit. Rev. Biochem, 15:291, 1984.
    • (1984) CRC Crit. Rev. Biochem , vol.15 , pp. 291
    • Bennett, W.S.1    Huber, R.2
  • 11
    • 0023488997 scopus 로고
    • Flexibility and rigidity, requirements of the function of proteins and protein pigment complexes
    • Huber, R. Flexibility and rigidity, requirements of the function of proteins and protein pigment complexes. Biochem. Soc. Trans., 15:1009-1020, 1987.
    • (1987) Biochem. Soc. Trans. , vol.15 , pp. 1009-1020
    • Huber, R.1
  • 13
    • 0028335096 scopus 로고
    • Structural mechanisms for domain movements in proteins
    • Gerstein, M., Lesk, A.M., Chothia, C. Structural mechanisms for domain movements in proteins. Biochemistry, 33(22):6739-6749, 1994.
    • (1994) Biochemistry , vol.33 , Issue.22 , pp. 6739-6749
    • Gerstein, M.1    Lesk, A.M.2    Chothia, C.3
  • 14
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett, M.J., Schlunegger, M.P., Eisenberg, D. 3D domain swapping: a mechanism for oligomer assembly. Prot. Sci., 4:2455-2468, 1995.
    • (1995) Prot. Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 15
    • 0031030767 scopus 로고    scopus 로고
    • Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation
    • Bernstein, B.E., Michels, P.A.M., Hol, WG. Synergistic effects of substrate-induced conformational changes in phosphoglycerate kinase activation. Nature 385:275-278, 1997.
    • (1997) Nature , vol.385 , pp. 275-278
    • Bernstein, B.E.1    Michels, P.A.M.2    Hol, W.G.3
  • 17
    • 0026536335 scopus 로고
    • Solution structure of a calmodulin-target peptide complex by multidimensional NMR
    • Ikura, M., Clore, G.M., Gronenborn, A.M., Zhu, G., Klee, C.B., Bax, A. Solution structure of a calmodulin-target peptide complex by multidimensional NMR. Science, 256: 632-637, 1992.
    • (1992) Science , vol.256 , pp. 632-637
    • Ikura, M.1    Clore, G.M.2    Gronenborn, A.M.3    Zhu, G.4    Klee, C.B.5    Bax, A.6
  • 18
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4Å structure of a calmodulin-peptide complex
    • Meador, W.E., Means, A.R., Quiocho, F.A. Target enzyme recognition by calmodulin: 2.4Å structure of a calmodulin-peptide complex. Science, 257:1251-1255, 1992.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 19
    • 0027759276 scopus 로고
    • Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures
    • Meador, WE., Means, A.R., Quiocho, F.A. Modulation of calmodulin plasticity in molecular recognition on the basis of X-ray structures. Science, 262:1718-1721, 1993.
    • (1993) Science , vol.262 , pp. 1718-1721
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 20
    • 0027528934 scopus 로고
    • Domain closure in adenylate kinase. Joints on either side of two helices close like neighboring fingers
    • Gerstein, M., Schulz, G., Chothia, C. Domain closure in adenylate kinase. Joints on either side of two helices close like neighboring fingers. J. Mol. Biol., 229:494-501, 1993.
    • (1993) J. Mol. Biol. , vol.229 , pp. 494-501
    • Gerstein, M.1    Schulz, G.2    Chothia, C.3
  • 21
    • 0025340754 scopus 로고
    • Induced-fit movements in adenylate kinases
    • Schulz, G.E., Muller, C.W., Diederichs, K. Induced-fit movements in adenylate kinases. J. Mol. Biol., 213:627-630, 1990.
    • (1990) J. Mol. Biol. , vol.213 , pp. 627-630
    • Schulz, G.E.1    Muller, C.W.2    Diederichs, K.3
  • 22
    • 0025273624 scopus 로고
    • Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins
    • Anderson, B.F., Baker, H.M., Norris, G.E., Rumball, S.V., Baker, E.N. Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins. Nature, 344:784-787, 1990.
    • (1990) Nature , vol.344 , pp. 784-787
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rumball, S.V.4    Baker, E.N.5
  • 23
    • 0001447664 scopus 로고
    • Transferrins: Insights into structures and function from studies of lactoferrin
    • Baker, E.N., Rumball, S.V., Anderson, B.F. Transferrins: insights into structures and function from studies of lactoferrin. Trends in Biochem. Sci., 12:350-353, 1987.
    • (1987) Trends in Biochem. Sci. , vol.12 , pp. 350-353
    • Baker, E.N.1    Rumball, S.V.2    Anderson, B.F.3
  • 24
    • 0027438949 scopus 로고
    • Domain closure in lactoferrin. Two hinges produce a see-saw motion between alternative close-packed interfaces
    • Gerstein, M., Anderson, B.F., Norris, G.E., Baker, E.N., Lesk, A.M., Chothia, C. Domain closure in lactoferrin. Two hinges produce a see-saw motion between alternative close-packed interfaces. J. Mol. Biol., 234:357-372, 1993.
    • (1993) J. Mol. Biol. , vol.234 , pp. 357-372
    • Gerstein, M.1    Anderson, B.F.2    Norris, G.E.3    Baker, E.N.4    Lesk, A.M.5    Chothia, C.6
  • 25
    • 0027235488 scopus 로고
    • Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding proteins with and without a ligand
    • Oh, B.H., Pandit, J., Kang, C.H., Nikaido, K., Gokcen, S., Ames, G.F.L., Kim, S.H. Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding proteins with and without a ligand. J. Bio. Chem., 268:11348-11355, 1993.
    • (1993) J. Bio. Chem. , vol.268 , pp. 11348-11355
    • Oh, B.H.1    Pandit, J.2    Kang, C.H.3    Nikaido, K.4    Gokcen, S.5    Ames, G.F.L.6    Kim, S.H.7
  • 26
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • Sharff, A.J., Rodseth, L.E., Spurlino, J.C., Quiocho. F.A. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry, 31:10657-10663, 1992.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 27
    • 0025754301 scopus 로고
    • The 2.3Å resolution structure of the maltose or maltodextrin binding protein, a primary receptor of bacterial transport and chemotaxis
    • Spurlino, J.C., Lu, G.Y., Quiocho, F.A. The 2.3Å resolution structure of the maltose or maltodextrin binding protein, a primary receptor of bacterial transport and chemotaxis. J. Bio. Chem., 266:5202-5219, 1991.
    • (1991) J. Bio. Chem. , vol.266 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.Y.2    Quiocho, F.A.3
  • 28
    • 0030444081 scopus 로고    scopus 로고
    • New structures of allosteric proteins revealing remarkable conformational changes
    • Mattevi, A., Rizzi, M., Bolognesi, M. New structures of allosteric proteins revealing remarkable conformational changes. Curr. Opin. Struct. Biol., 6:824-829, 1996.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 824-829
    • Mattevi, A.1    Rizzi, M.2    Bolognesi, M.3
  • 29
    • 0014958182 scopus 로고
    • Stereochemistry of cooperative effects in hemoglobin
    • Perutz, M.F. Stereochemistry of cooperative effects in hemoglobin. Nature, 228:727-734, 1970.
    • (1970) Nature , vol.228 , pp. 727-734
    • Perutz, M.F.1
  • 30
    • 0024322304 scopus 로고
    • The allosteric transition of glycogen phosphorylase
    • Barford, D., Johnson, L.N. The allosteric transition of glycogen phosphorylase. Nature, 340:609-616, 1989.
    • (1989) Nature , vol.340 , pp. 609-616
    • Barford, D.1    Johnson, L.N.2
  • 31
    • 0029867028 scopus 로고    scopus 로고
    • Crystal structure of the t state of allosteric yeast chorismate mutase and comparison with the r state
    • Stråter, N., Håkansson, K., Schnappauf, G., Braus, G., Lipscomb, W.N. Crystal structure of the t state of allosteric yeast chorismate mutase and comparison with the r state. Proc. Natl. Acad. Sci. USA, 93:3330-3334, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3330-3334
    • Stråter, N.1    Håkansson, K.2    Schnappauf, G.3    Braus, G.4    Lipscomb, W.N.5
  • 32
    • 0001858251 scopus 로고
    • Application of a theory of enzyme specificity to protein-synthesis
    • Koshland, D.E. Application of a theory of enzyme specificity to protein-synthesis. Proc. Natl. Acad. Sci. USA, 44:98, 1958.
    • (1958) Proc. Natl. Acad. Sci. USA , vol.44 , pp. 98
    • Koshland, D.E.1
  • 33
    • 0026425975 scopus 로고
    • Rusting the lock and key model for protein-ligand binding
    • Jorgensen, W.L. Rusting the lock and key model for protein-ligand binding. Science, 254:954-955, 1991.
    • (1991) Science , vol.254 , pp. 954-955
    • Jorgensen, W.L.1
  • 34
    • 0030883755 scopus 로고    scopus 로고
    • Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates
    • Wriggers, W., Schulten, K. Protein domain movements: Detection of rigid domains and visualization of hinges in comparisons of atomic coordinates. Proteins 29:1-14, 1997.
    • (1997) Proteins , vol.29 , pp. 1-14
    • Wriggers, W.1    Schulten, K.2
  • 35
    • 0030939896 scopus 로고    scopus 로고
    • A new method for modeling large-scale rearrangements of protein domains
    • Maiorov, V., Abagyan, R. A new method for modeling large-scale rearrangements of protein domains. Proteins 27:410-424, 1997.
    • (1997) Proteins , vol.27 , pp. 410-424
    • Maiorov, V.1    Abagyan, R.2
  • 36
    • 0028956684 scopus 로고
    • Dramatic differences in the motions of the mouth of open and closed cytochrome p450bm-3 by molecular dynamic simulations
    • Paulsen, M.D., Orenstein, R.L. Dramatic differences in the motions of the mouth of open and closed cytochrome p450bm-3 by molecular dynamic simulations. Proteins 21:237-243, 1995.
    • (1995) Proteins , vol.21 , pp. 237-243
    • Paulsen, M.D.1    Orenstein, R.L.2
  • 38
    • 84986467005 scopus 로고
    • Conformational analysis of flexible ligands in macromolecular receptor sites
    • Leach, A.R., Kuntz, I.D. Conformational analysis of flexible ligands in macromolecular receptor sites. J. Comp. Chem., 13(6):730-748, 1992.
    • (1992) J. Comp. Chem. , vol.13 , Issue.6 , pp. 730-748
    • Leach, A.R.1    Kuntz, I.D.2
  • 39
    • 84988128979 scopus 로고
    • Geometrically feasible binding modes of a flexible ligand molecule at the receptor site
    • Ghose, A.K., Crippen, G.M. Geometrically feasible binding modes of a flexible ligand molecule at the receptor site. J. Comp. Chem., 6:350-359, 1985.
    • (1985) J. Comp. Chem. , vol.6 , pp. 350-359
    • Ghose, A.K.1    Crippen, G.M.2
  • 40
    • 0025135112 scopus 로고
    • Automated docking of substrates to proteins by simulated annealing
    • Goodsell, D.S., Olson, A.J. Automated docking of substrates to proteins by simulated annealing. Proteins, 8:195, 1990.
    • (1990) Proteins , vol.8 , pp. 195
    • Goodsell, D.S.1    Olson, A.J.2
  • 41
    • 0027985242 scopus 로고
    • Rational automatic search method for stable docking models of protein and ligand
    • Mizutani, M.Y., Tomioka, N., Itai, A. Rational automatic search method for stable docking models of protein and ligand. J. Mol. Biol., 243:310-326, 1994.
    • (1994) J. Mol. Biol. , vol.243 , pp. 310-326
    • Mizutani, M.Y.1    Tomioka, N.2    Itai, A.3
  • 42
    • 84986492468 scopus 로고
    • Flexible ligand docking without parameter adjustment across four ligand receptor complexes
    • Clark, K.P., Ajay. Flexible ligand docking without parameter adjustment across four ligand receptor complexes. J. Comp. Chem., 16:1210-1226, 1995.
    • (1995) J. Comp. Chem. , vol.16 , pp. 1210-1226
    • Clark, K.P.1    Ajay2
  • 44
    • 0030154893 scopus 로고    scopus 로고
    • Hammerhead: Fast, fully automated docking of flexible ligands to protein binding sites
    • Welch, W., Ruppert, J., Jain, A.N. Hammerhead: fast, fully automated docking of flexible ligands to protein binding sites. Chem. Biol., 3:449-462, 1996.
    • (1996) Chem. Biol. , vol.3 , pp. 449-462
    • Welch, W.1    Ruppert, J.2    Jain, A.N.3
  • 45
    • 0030599010 scopus 로고    scopus 로고
    • A fast flexible docking method using incremental construction algorithm
    • Rarey, M., Kramer, B., Lengauer, T., Klebe, G. A fast flexible docking method using incremental construction algorithm. J. Mol. Biol., 261:470-489, 1996.
    • (1996) J. Mol. Biol. , vol.261 , pp. 470-489
    • Rarey, M.1    Kramer, B.2    Lengauer, T.3    Klebe, G.4
  • 46
    • 0031581852 scopus 로고    scopus 로고
    • Molecular docking to ensembles of protein structures
    • Knegtel, R.M.A., Kuntz, I.D., Oshiro, C.M. Molecular docking to ensembles of protein structures. J. Mol. Biol., 266:424-440, 1997.
    • (1997) J. Mol. Biol. , vol.266 , pp. 424-440
    • Knegtel, R.M.A.1    Kuntz, I.D.2    Oshiro, C.M.3
  • 47
    • 0031552362 scopus 로고    scopus 로고
    • Development and validation of a genetic algorithm for flexible docking
    • Jones, G., Willett, P., Glen, R.C., Leach, A.R., Taylor, R. Development and validation of a genetic algorithm for flexible docking. J. Mol. Biol., 267:727-748, 1997.
    • (1997) J. Mol. Biol. , vol.267 , pp. 727-748
    • Jones, G.1    Willett, P.2    Glen, R.C.3    Leach, A.R.4    Taylor, R.5
  • 48
    • 0028158936 scopus 로고
    • Ligand docking to proteins with discrete side-chain flexibility
    • Leach, A.R. Ligand docking to proteins with discrete side-chain flexibility. J. Mol. Biol., 235:345-356, 1994.
    • (1994) J. Mol. Biol. , vol.235 , pp. 345-356
    • Leach, A.R.1
  • 49
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones, G., Willet, P., Glen, R.C. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J. Mol. Biol., 245:43-53, 1995.
    • (1995) J. Mol. Biol. , vol.245 , pp. 43-53
    • Jones, G.1    Willet, P.2    Glen, R.C.3
  • 50
    • 0028940058 scopus 로고
    • An automated Computer-Vision & Robotics based technique for 3-D flexible biomolecular docking and matching
    • Sandak, B., Nussinov, R., Wolfson, H.J. An automated Computer-Vision & Robotics based technique for 3-D flexible biomolecular docking and matching. Computer Applications in the Biosciences, 11:87-99, 1995.
    • (1995) Computer Applications in the Biosciences , vol.11 , pp. 87-99
    • Sandak, B.1    Nussinov, R.2    Wolfson, H.J.3
  • 51
    • 0009407367 scopus 로고    scopus 로고
    • Hinge-bending at molecular interfaces: Automated docking of a dihydroxyethylene-containing inhibitor of the HIV-1 protease
    • Sarma, R.H., Sarma, M.H. (eds). New York: Adenine Press
    • Sandak, B., Wolfson, H.J., Nussinov, R. Hinge-bending at molecular interfaces: Automated docking of a dihydroxyethylene-containing inhibitor of the HIV-1 protease. In: "Journal of Biomolecular Structure & Dynamics, Vol 1, Proceedings of the Ninth Conversation." Sarma, R.H., Sarma, M.H. (eds). New York: Adenine Press, 1996:233-252.
    • (1996) Journal of Biomolecular Structure & Dynamics, Vol 1, Proceedings of the Ninth Conversation , vol.1 , pp. 233-252
    • Sandak, B.1    Wolfson, H.J.2    Nussinov, R.3
  • 52
    • 0026301147 scopus 로고
    • Generalizing the generalized Hough transform
    • Wolfson, H.J. Generalizing the generalized Hough transform. Pattern Recognition Letters, 12(9):565-573, 1991.
    • (1991) Pattern Recognition Letters , vol.12 , Issue.9 , pp. 565-573
    • Wolfson, H.J.1
  • 56
    • 0027976930 scopus 로고
    • Molecular surface representation by sparse critical points
    • Lin, S.L., Nussinov, R., Fischer, D., Wolfson, H.J. Molecular surface representation by sparse critical points. Proteins 18:94-101, 1994.
    • (1994) Proteins , vol.18 , pp. 94-101
    • Lin, S.L.1    Nussinov, R.2    Fischer, D.3    Wolfson, H.J.4
  • 57
    • 0030130449 scopus 로고    scopus 로고
    • Molecular recognition via the face center representation of molecular surface
    • Lin, S.L., Nussinov, R. Molecular recognition via the face center representation of molecular surface. J. Mol. Graphics, 14:78-97, 1996.
    • (1996) J. Mol. Graphics , vol.14 , pp. 78-97
    • Lin, S.L.1    Nussinov, R.2
  • 58
    • 0021107965 scopus 로고
    • Solvent-accessible surfaces of proteins and nucleic acids
    • Connolly, M.L. Solvent-accessible surfaces of proteins and nucleic acids. Science, 221:709-713, 1983.
    • (1983) Science , vol.221 , pp. 709-713
    • Connolly, M.L.1
  • 59
    • 0000538815 scopus 로고
    • Analytical molecular surface calculation
    • Connolly, M.L. Analytical molecular surface calculation. J. Appl. Cryst., 16:548-558, 1983.
    • (1983) J. Appl. Cryst. , vol.16 , pp. 548-558
    • Connolly, M.L.1
  • 60
    • 0017429069 scopus 로고
    • Areas, volumes, packing and protein structure
    • Richards, F.M. Areas, volumes, packing and protein structure. Ann. Rev. Biophys. Bioeng., 6:151-176, 1977.
    • (1977) Ann. Rev. Biophys. Bioeng. , vol.6 , pp. 151-176
    • Richards, F.M.1
  • 62
    • 0029823282 scopus 로고    scopus 로고
    • Rational choice of molecular dynamics simulation parameters through the use of the three-dimensional autocorrelation method: Application to calmodulin flexibility study
    • Yasri, A., Chiche, L., Haiech, J., Grassy, G. Rational choice of molecular dynamics simulation parameters through the use of the three-dimensional autocorrelation method: application to calmodulin flexibility study. Prot. Eng., 9:959-976, 1996.
    • (1996) Prot. Eng. , vol.9 , pp. 959-976
    • Yasri, A.1    Chiche, L.2    Haiech, J.3    Grassy, G.4
  • 63
  • 64
    • 0025785057 scopus 로고
    • Protein Docking and Complementarity
    • Shoichet, B.K., Kuntz, I.D. Protein Docking and Complementarity. J. Mol. Biol., 221:327-346, 1991.
    • (1991) J. Mol. Biol. , vol.221 , pp. 327-346
    • Shoichet, B.K.1    Kuntz, I.D.2
  • 65
    • 0027385177 scopus 로고
    • Matching chemistry and shape in molecular docking
    • Shoichet, B.K., Kuntz, I.D. Matching chemistry and shape in molecular docking. Protein Engineering, 6:723-732, 1993.
    • (1993) Protein Engineering , vol.6 , pp. 723-732
    • Shoichet, B.K.1    Kuntz, I.D.2


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