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Volumn 56, Issue 1, 2004, Pages 93-101

A physical reference state unifies the structure-derived potential of mean force for protein folding and binding

Author keywords

Binding stability; Docking decoys; Energy score functions; Knowledge based potential; Potential of mean force; Reference state

Indexed keywords

PROTEIN;

EID: 2642524483     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20019     Document Type: Article
Times cited : (177)

References (78)
  • 2
    • 0036882094 scopus 로고    scopus 로고
    • Development of a polarizable force field for proteins via ab initio quantum chemistry: First generation model and gas phase tests
    • Kaminski GA, Stern HA, Berne BJ, Friesner R. Development of a polarizable force field for proteins via ab initio quantum chemistry: first generation model and gas phase tests. J Comp Chem 2002;23:1515-1531.
    • (2002) J Comp Chem , vol.23 , pp. 1515-1531
    • Kaminski, G.A.1    Stern, H.A.2    Berne, B.J.3    Friesner, R.4
  • 3
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • Lazaridis T, Karplus M. Effective energy function for proteins in solution. Proteins 1999;35:133-152.
    • (1999) Proteins , vol.35 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 4
    • 0017021957 scopus 로고
    • Medium- and long-range interaction parameters between amino acids for predicting three-dimensional structures of proteins
    • Tanaka S, Scheraga HA. Medium- and long-range interaction parameters between amino acids for predicting three-dimensional structures of proteins. Macromolecules 1976;9:945-950.
    • (1976) Macromolecules , vol.9 , pp. 945-950
    • Tanaka, S.1    Scheraga, H.A.2
  • 5
    • 0025341310 scopus 로고
    • Calculation of conformational ensembles from potentials of mean force: An approach to the knowledge-based prediction of local structures in globular proteins
    • Sippl MJ. Calculation of conformational ensembles from potentials of mean force: an approach to the knowledge-based prediction of local structures in globular proteins. J Mol Biol 1990;213:859-883.
    • (1990) J Mol Biol , vol.213 , pp. 859-883
    • Sippl, M.J.1
  • 6
    • 0029976427 scopus 로고    scopus 로고
    • Statistical potentials extracted from protein structures: How accurate are they?
    • Thomas PD, Dill KA. Statistical potentials extracted from protein structures: how accurate are they? J Mol Biol 1996;257:457-469.
    • (1996) J Mol Biol , vol.257 , pp. 457-469
    • Thomas, P.D.1    Dill, K.A.2
  • 7
    • 0031891022 scopus 로고    scopus 로고
    • Computation of electrostatic complements to proteins: A case of charge stabilized binding
    • Chong LT, Dempster SE, Hendsch ZS, Lee L-P, Tidor B. Computation of electrostatic complements to proteins: a case of charge stabilized binding. Protein Sci 1998;7:206-210.
    • (1998) Protein Sci , vol.7 , pp. 206-210
    • Chong, L.T.1    Dempster, S.E.2    Hendsch, Z.S.3    Lee, L.-P.4    Tidor, B.5
  • 8
    • 0034602373 scopus 로고    scopus 로고
    • Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model
    • Wang W, Kollman PA. Free energy calculations on dimer stability of the HIV protease using molecular dynamics and a continuum solvent model. J Mol Biol 2000;303:567-582.
    • (2000) J Mol Biol , vol.303 , pp. 567-582
    • Wang, W.1    Kollman, P.A.2
  • 9
    • 0034039797 scopus 로고    scopus 로고
    • Electrostatics aspects of protein-protein interactions
    • Sheinerman F, Norel R, Honig B. Electrostatics aspects of protein-protein interactions. Curr Opin Struct Biol 2000; 10:153-159.
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 153-159
    • Sheinerman, F.1    Norel, R.2    Honig, B.3
  • 10
    • 0037470581 scopus 로고    scopus 로고
    • An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes
    • Kortemme T, Morozov A, Baker D. An orientation-dependent hydrogen bonding potential improves prediction of specificity and structure for proteins and protein-protein complexes. J Mol Biol 2003;326:1239-1259.
    • (2003) J Mol Biol , vol.326 , pp. 1239-1259
    • Kortemme, T.1    Morozov, A.2    Baker, D.3
  • 11
    • 0037340493 scopus 로고    scopus 로고
    • Development of unified statistical potentials describing protein-protein interactions
    • Lu H, Lu L, Skolnick J. Development of unified statistical potentials describing protein-protein interactions. Biophys J 2003; 84:1895-1901.
    • (2003) Biophys J , vol.84 , pp. 1895-1901
    • Lu, H.1    Lu, L.2    Skolnick, J.3
  • 12
    • 0035342450 scopus 로고    scopus 로고
    • Residue frequencies and pairing preferences at protein-protein interfaces
    • Glaser F, Sternberg D, Vakser I, Ben-Tal N. Residue frequencies and pairing preferences at protein-protein interfaces. Proteins 2001;43:89-102.
    • (2001) Proteins , vol.43 , pp. 89-102
    • Glaser, F.1    Sternberg, D.2    Vakser, I.3    Ben-Tal, N.4
  • 13
    • 0037229456 scopus 로고    scopus 로고
    • Analyzing six types of protein-protein complexes
    • Ofran Y, Rost B. Analyzing six types of protein-protein complexes. J Mol Biol 2003;325:377-387.
    • (2003) J Mol Biol , vol.325 , pp. 377-387
    • Ofran, Y.1    Rost, B.2
  • 14
    • 0033562633 scopus 로고    scopus 로고
    • Use of pair potentials across protein interfaces in screening predicted docked complexes
    • Moont G, Gabb H, Sternberg M. Use of pair potentials across protein interfaces in screening predicted docked complexes. Proteins 1999;35:364-373.
    • (1999) Proteins , vol.35 , pp. 364-373
    • Moont, G.1    Gabb, H.2    Sternberg, M.3
  • 15
    • 0032515101 scopus 로고    scopus 로고
    • A soft, mean field potential derived from crystal contacts for predicting protein-protein interactions
    • Robert C, Janin J. A soft, mean field potential derived from crystal contacts for predicting protein-protein interactions. J Mol Biol 1998;283:1037-1047.
    • (1998) J Mol Biol , vol.283 , pp. 1037-1047
    • Robert, C.1    Janin, J.2
  • 16
    • 0000823044 scopus 로고    scopus 로고
    • BLEEP-potential of mean force describing protein-ligand interactions: I. Generating potential
    • Mitchell JBO, Laskowski RA, Alex A, Thornton JM. BLEEP-potential of mean force describing protein-ligand interactions: I. Generating potential. J Comp Chem 1999;20:1165-1176.
    • (1999) J Comp Chem , vol.20 , pp. 1165-1176
    • Mitchell, J.B.O.1    Laskowski, R.A.2    Alex, A.3    Thornton, J.M.4
  • 17
    • 0034308172 scopus 로고    scopus 로고
    • Discriminating between homodimeric and monomeric proteins in the crystalline state
    • Ponstingl H, Henrick K, Thornton J. Discriminating between homodimeric and monomeric proteins in the crystalline state. Proteins 2000;41:47-57.
    • (2000) Proteins , vol.41 , pp. 47-57
    • Ponstingl, H.1    Henrick, K.2    Thornton, J.3
  • 18
    • 0036467249 scopus 로고    scopus 로고
    • Potential of mean force for protein-protein interaction studies
    • Jiang L, Gao Y, Mao F, Liu Z, Lai L. Potential of mean force for protein-protein interaction studies. Proteins 2002;46:190-196.
    • (2002) Proteins , vol.46 , pp. 190-196
    • Jiang, L.1    Gao, Y.2    Mao, F.3    Liu, Z.4    Lai, L.5
  • 19
    • 0032488962 scopus 로고    scopus 로고
    • An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction
    • Samudrala R, Moult J. An all-atom distance-dependent conditional probability discriminatory function for protein structure prediction. J Mol Biol 1998;275:895-916.
    • (1998) J Mol Biol , vol.275 , pp. 895-916
    • Samudrala, R.1    Moult, J.2
  • 20
    • 0035882533 scopus 로고    scopus 로고
    • A distance-dependent atomic knowledge-based potential for improved protein structure selection
    • Lu H, Skolnick J. A distance-dependent atomic knowledge-based potential for improved protein structure selection. Proteins 2001; 44:223-232.
    • (2001) Proteins , vol.44 , pp. 223-232
    • Lu, H.1    Skolnick, J.2
  • 21
    • 0041509110 scopus 로고    scopus 로고
    • Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction
    • Zhou H, Zhou Y. Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci 2002;11:2714-2726; 2003;12:2121.
    • (2003) Protein Sci , vol.12 , pp. 2121
    • Zhou, H.1    Zhou, Y.2
  • 22
    • 0036838311 scopus 로고    scopus 로고
    • Zhou H, Zhou Y. Distance-scaled, finite ideal-gas reference state improves structure-derived potentials of mean force for structure selection and stability prediction. Protein Sci 2002;11:2714-2726; 2003;12:2121.
    • (2002) Protein Sci , vol.11 , pp. 2714-2726
  • 23
    • 0345827721 scopus 로고    scopus 로고
    • Quantifying the effect of burial of amino acid residues on protein stability
    • Zhou H, Zhou Y. Quantifying the effect of burial of amino acid residues on protein stability. Proteins 2004;54:315-322.
    • (2004) Proteins , vol.54 , pp. 315-322
    • Zhou, H.1    Zhou, Y.2
  • 24
    • 0037110589 scopus 로고    scopus 로고
    • Multiprospector: An algorithm for the prediction of protein-protein interactions by multimeric threading
    • Lu L, Lu H, Skolnick J. Multiprospector: an algorithm for the prediction of protein-protein interactions by multimeric threading. Proteins 2002;49:350-364.
    • (2002) Proteins , vol.49 , pp. 350-364
    • Lu, L.1    Lu, H.2    Skolnick, J.3
  • 26
    • 0034663658 scopus 로고    scopus 로고
    • Scoring docked conformations generated by rigid-body protein-protein docking
    • Camacho CJ, Gatchell DW, Kimura SR, Vajda S. Scoring docked conformations generated by rigid-body protein-protein docking. Proteins 2000;40:525-537.
    • (2000) Proteins , vol.40 , pp. 525-537
    • Camacho, C.J.1    Gatchell, D.W.2    Kimura, S.R.3    Vajda, S.4
  • 27
    • 0242299207 scopus 로고    scopus 로고
    • Atomic contact vectors in protein-protein recognition
    • Mintseris J, Weng Z. Atomic contact vectors in protein-protein recognition. Proteins 2003;53:629-639.
    • (2003) Proteins , vol.53 , pp. 629-639
    • Mintseris, J.1    Weng, Z.2
  • 28
    • 0035853028 scopus 로고    scopus 로고
    • Identification of protein oligomerization states by analysis of interface conservation
    • Elock A, McCammon J. Identification of protein oligomerization states by analysis of interface conservation. Proc Natl Acad Sci USA 2001;98:2990-2994.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2990-2994
    • Elock, A.1    McCammon, J.2
  • 29
    • 0031058541 scopus 로고    scopus 로고
    • The statistical-thermodynamic basis for computation of binding affinities: A critical review
    • Gilson MK, Given JA, Bush BL, McCammon JA. The statistical-thermodynamic basis for computation of binding affinities: a critical review. Biophys J 1997;72:1047-1069.
    • (1997) Biophys J , vol.72 , pp. 1047-1069
    • Gilson, M.K.1    Given, J.A.2    Bush, B.L.3    McCammon, J.A.4
  • 30
    • 0036677555 scopus 로고    scopus 로고
    • On the calculation of absolute macromolecular binding free energies
    • Luo H, Sharp K. On the calculation of absolute macromolecular binding free energies. Proc Natl Acad Sci USA 2003;99:10399-10404.
    • (2003) Proc Natl Acad Sci USA , vol.99 , pp. 10399-10404
    • Luo, H.1    Sharp, K.2
  • 31
    • 0000882405 scopus 로고    scopus 로고
    • BLEEP potential of mean force describing protein-ligand interactions: II. Calculation of binding energies and comparison with experimental data
    • Mitchell JBO, Laskowski RA, Alex A, Foster MJ, Thornton JM. BLEEP potential of mean force describing protein-ligand interactions: II. Calculation of binding energies and comparison with experimental data. J Comp Chem 1999;20:1177-1185.
    • (1999) J Comp Chem , vol.20 , pp. 1177-1185
    • Mitchell, J.B.O.1    Laskowski, R.A.2    Alex, A.3    Foster, M.J.4    Thornton, J.M.5
  • 32
    • 0027087369 scopus 로고
    • Calculation of the free energy of association for protein complexes
    • Horton N, Lewis M. Calculation of the free energy of association for protein complexes. Protein Sci 1992;1:169-181.
    • (1992) Protein Sci , vol.1 , pp. 169-181
    • Horton, N.1    Lewis, M.2
  • 33
    • 0028102849 scopus 로고
    • Effect of conformational flexibility and solvation on receptor-ligand binding free energies
    • Vajda S, Weng Z, Rosenfeld R, Delisi C. Effect of conformational flexibility and solvation on receptor-ligand binding free energies. Biochemistry 1994;33:13977-13988.
    • (1994) Biochemistry , vol.33 , pp. 13977-13988
    • Vajda, S.1    Weng, Z.2    Rosenfeld, R.3    Delisi, C.4
  • 34
    • 0031561809 scopus 로고    scopus 로고
    • Protein binding versus protein folding: The role of hydrophilic bridges in protein associations
    • Xu D, Lin SL, Nussinov R. Protein binding versus protein folding: the role of hydrophilic bridges in protein associations. J Mol Biol 1997;265:68-84.
    • (1997) J Mol Biol , vol.265 , pp. 68-84
    • Xu, D.1    Lin, S.L.2    Nussinov, R.3
  • 35
    • 0036893044 scopus 로고    scopus 로고
    • The stability scale and atomic solvation parameters extracted from 1023 mutation experiments
    • Zhou H, Zhou Y. The stability scale and atomic solvation parameters extracted from 1023 mutation experiments. Proteins 2002;49: 483-492.
    • (2002) Proteins , vol.49 , pp. 483-492
    • Zhou, H.1    Zhou, Y.2
  • 36
    • 23044531267 scopus 로고    scopus 로고
    • Protein recognition by sequence-to-structure fitness: Bridging efficiency and capacity of threading models
    • Meller J, Elber R. Protein recognition by sequence-to-structure fitness: bridging efficiency and capacity of threading models. Adv Chem Phys 2002;120:77-130.
    • (2002) Adv Chem Phys , vol.120 , pp. 77-130
    • Meller, J.1    Elber, R.2
  • 37
    • 2542631929 scopus 로고    scopus 로고
    • Single body knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition
    • Forthcoming
    • Zhou H, Zhou Y. Single body knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition. Proteins 2004. Forthcoming.
    • (2004) Proteins
    • Zhou, H.1    Zhou, Y.2
  • 38
    • 0036468385 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions by docking methods
    • Smith GR, Sternberg MJE. Prediction of protein-protein interactions by docking methods. Curr Opin Struct Biol 2002;12:28-35.
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 28-35
    • Smith, G.R.1    Sternberg, M.J.E.2
  • 39
    • 0017667829 scopus 로고
    • Thermodynamics of gelation of sickle cell deoxyhemoglobin
    • Ross PD, Hofrichter J, Eaton WA. Thermodynamics of gelation of sickle cell deoxyhemoglobin. J Mol Biol 1977; 115:111-134.
    • (1977) J Mol Biol , vol.115 , pp. 111-134
    • Ross, P.D.1    Hofrichter, J.2    Eaton, W.A.3
  • 40
    • 0032424250 scopus 로고    scopus 로고
    • How and why phosphotyrosine-containing peptides bind to the SH2 and PTB domains
    • Zhou Y, Abagyan AR. How and why phosphotyrosine-containing peptides bind to the SH2 and PTB domains. Fold Des 1998;3:513-522.
    • (1998) Fold Des , vol.3 , pp. 513-522
    • Zhou, Y.1    Abagyan, A.R.2
  • 42
    • 0037168045 scopus 로고    scopus 로고
    • Comparative binding energy (COMBINE) analysis of oppA-peptide complexes to relate structure to binding thermodynamics
    • Wang T, Wade RC. Comparative binding energy (COMBINE) analysis of oppA-peptide complexes to relate structure to binding thermodynamics. J Med Chem 2002;45:4828-4837.
    • (2002) J Med Chem , vol.45 , pp. 4828-4837
    • Wang, T.1    Wade, R.C.2
  • 43
    • 0017277533 scopus 로고
    • Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz)
    • Vincent JP, Lazdunski M. Pre-existence of the active site in zymogens, the interaction of trypsinogen with the basic pancreatic trypsin inhibitor (Kunitz). FEBS Lett 1976;63:240-244.
    • (1976) FEBS Lett , vol.63 , pp. 240-244
    • Vincent, J.P.1    Lazdunski, M.2
  • 44
    • 0027139338 scopus 로고
    • Affinity and specificity of serine endopeptidase-protein inhibitor interactions: Empirical free energy calculations based on X-ray crystallographic structures
    • Krystek S, Stouch T, Novonty J. Affinity and specificity of serine endopeptidase-protein inhibitor interactions: empirical free energy calculations based on X-ray crystallographic structures. J Mol Biol 1993;234:661-679.
    • (1993) J Mol Biol , vol.234 , pp. 661-679
    • Krystek, S.1    Stouch, T.2    Novonty, J.3
  • 45
    • 0141506108 scopus 로고    scopus 로고
    • Protein Ligand Database (PLD): Additional understanding of the nature and specificity of protein-ligand complexes
    • Puvanendrampillai D, Mitchell J. Protein Ligand Database (PLD): Additional understanding of the nature and specificity of protein-ligand complexes. Bioinformatics 2003;19:1856-1857.
    • (2003) Bioinformatics , vol.19 , pp. 1856-1857
    • Puvanendrampillai, D.1    Mitchell, J.2
  • 46
    • 0028227795 scopus 로고
    • N9 neuraminidase complexes with antibodies NC41 and NC10: Empirical free energy calculations capture specificity trends observed with mutant binding data
    • Tulip WR, Harley VR, Webster RG, Novotny J. N9 neuraminidase complexes with antibodies NC41 and NC10: empirical free energy calculations capture specificity trends observed with mutant binding data. Biochemistry 1994;33:7986-7997.
    • (1994) Biochemistry , vol.33 , pp. 7986-7997
    • Tulip, W.R.1    Harley, V.R.2    Webster, R.G.3    Novotny, J.4
  • 49
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpEbound to the ATPase domain of the molecular chaperone DnaK
    • Harrison CJ, HayerHartl M, DiLiberto M, Hartl FU, Kuriyan J. Crystal structure of the nucleotide exchange factor GrpEbound to the ATPase domain of the molecular chaperone DnaK. Science 1997;276:431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    HayerHartl, M.2    DiLiberto, M.3    Hartl, F.U.4    Kuriyan, J.5
  • 50
    • 0030575866 scopus 로고    scopus 로고
    • Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2
    • Gorina S, Pavletich NP. Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. Science 1996;274:1001-1005.
    • (1996) Science , vol.274 , pp. 1001-1005
    • Gorina, S.1    Pavletich, N.P.2
  • 51
    • 0025818824 scopus 로고
    • Synthetic peptides as the basis for vaccine design
    • Arnon R. Synthetic peptides as the basis for vaccine design. Mol Immunol 1991;28:209-215.
    • (1991) Mol Immunol , vol.28 , pp. 209-215
    • Arnon, R.1
  • 52
    • 0023920595 scopus 로고
    • Reshaping human antibodies: Grafting an antilysozyme activity
    • Verhoeyen M, Milstein C, Winter G. Reshaping human antibodies: grafting an antilysozyme activity. Science 1988;239:1534-1536.
    • (1988) Science , vol.239 , pp. 1534-1536
    • Verhoeyen, M.1    Milstein, C.2    Winter, G.3
  • 53
    • 0032584775 scopus 로고    scopus 로고
    • Determination of the binding constants for three HPr-specific monoclonal antibodies and their fab fragments
    • Smallshaw JE, Brokx S, Lee JS, Waygood EB. Determination of the binding constants for three HPr-specific monoclonal antibodies and their fab fragments. J Mol Biol 1998;325:765-774.
    • (1998) J Mol Biol , vol.325 , pp. 765-774
    • Smallshaw, J.E.1    Brokx, S.2    Lee, J.S.3    Waygood, E.B.4
  • 55
    • 0343494918 scopus 로고    scopus 로고
    • Crystal structure of the conserved core of HIV-1 Nef complexed with a src family SH3 domain
    • Lee CH, Saksela K, Mirza UA, Chait BT, Kuriyan J. Crystal structure of the conserved core of HIV-1 Nef complexed with a src family SH3 domain. Cell 1996;85:931-942.
    • (1996) Cell , vol.85 , pp. 931-942
    • Lee, C.H.1    Saksela, K.2    Mirza, U.A.3    Chait, B.T.4    Kuriyan, J.5
  • 56
    • 20644435471 scopus 로고
    • Carboxypeptidase inhibitor from potatoes
    • Hass GM, Ryan CA. Carboxypeptidase inhibitor from potatoes. Methods Enzymol 1981;80:779-790.
    • (1981) Methods Enzymol , vol.80 , pp. 779-790
    • Hass, G.M.1    Ryan, C.A.2
  • 58
    • 0026034095 scopus 로고
    • The antigenic surface of staphylococcal nuclease: 2. Analysis of the n-1 epitope by site-directed mutagenesis
    • Smith AM, Benjamin DC. The antigenic surface of staphylococcal nuclease: 2. Analysis of the n-1 epitope by site-directed mutagenesis. J Immunol 1991;146:1259-1264.
    • (1991) J Immunol , vol.146 , pp. 1259-1264
    • Smith, A.M.1    Benjamin, D.C.2
  • 59
    • 0018375671 scopus 로고
    • Inhibition of porcine glandular kallikreins by structurally homologous proteinase inhibitor of the Kunitz type
    • Dietl T, Huber C, Geiger R, Iwanaga S, Fritz H. Inhibition of porcine glandular kallikreins by structurally homologous proteinase inhibitor of the Kunitz type. Hoppe-Seyler's Z Physiol Chem 1979;360:67-71.
    • (1979) Hoppe-Seyler's Z Physiol Chem , vol.360 , pp. 67-71
    • Dietl, T.1    Huber, C.2    Geiger, R.3    Iwanaga, S.4    Fritz, H.5
  • 60
    • 0018173019 scopus 로고
    • -10m for the subtilisin BPN'-protein proteinase inhibitor (Streptomyces subtilisin inhibitor) complex by a single photon counting technique
    • -10m for the subtilisin BPN'-protein proteinase inhibitor (Streptomyces subtilisin inhibitor) complex by a single photon counting technique. J Biochem 1978;84:1195-1202.
    • (1978) J Biochem , vol.84 , pp. 1195-1202
    • Uehara, Y.1    Tonomura, B.2    Hiromi, K.3
  • 61
    • 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 residues
    • Bigler TL, Lu W, Park SJ, Tashiro M, Wieczorek M, Wynn R, Laskowski MJ. Binding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded residues. Protein Sci 1993;2:786-799.
    • (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.J.7
  • 62
    • 0026056921 scopus 로고
    • Streptococal protein G gene structure and protein bind properties
    • Sjobring U, Bjorek L, Kastern W. Streptococal protein G gene structure and protein bind properties. J Biol Chem 1991;266:399-405.
    • (1991) J Biol Chem , vol.266 , pp. 399-405
    • Sjobring, U.1    Bjorek, L.2    Kastern, W.3
  • 63
    • 0028174260 scopus 로고
    • Glu192 ← Gln substitution in thrombin yields an enzyme that is effectively inhibited by bovine pancreatic trypsin inhibitor and tissue factor pathway inhibitor
    • Guinto ER, Ye J, Bonniec BFL, Esmon CT. Glu192 ← Gln substitution in thrombin yields an enzyme that is effectively inhibited by bovine pancreatic trypsin inhibitor and tissue factor pathway inhibitor. J Biol Chem 1994;269:18395-18400.
    • (1994) J Biol Chem , vol.269 , pp. 18395-18400
    • Guinto, E.R.1    Ye, J.2    Bonniec, B.F.L.3    Esmon, C.T.4
  • 64
    • 0000765963 scopus 로고
    • Eglin elastase-cathepsing inhibitor from leeches
    • Seemuller U, Fritz H, Euliz M. Eglin elastase-cathepsing inhibitor from leeches. Methods Enzymol 1981;80:804-816.
    • (1981) Methods Enzymol , vol.80 , pp. 804-816
    • Seemuller, U.1    Fritz, H.2    Euliz, M.3
  • 65
  • 66
    • 0024431034 scopus 로고
    • The refined 1.9 angstroms crystal structure of human alpha-thrombin: Interaction with D-PHE-PRO-ARG chloromethylketone and significance of the TYR-PRO-PRO-TRP insertion segment
    • Bode W, Mayr I, Baumann U, Huber R, Stone S, Hofsteenge J. The refined 1.9 angstroms crystal structure of human alpha-thrombin: interaction with D-PHE-PRO-ARG chloromethylketone and significance of the TYR-PRO-PRO-TRP insertion segment. EMBO J 1989;8:3467-3475.
    • (1989) EMBO J , vol.8 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.5    Hofsteenge, J.6
  • 67
    • 0026598960 scopus 로고
    • Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex
    • Vos AD, Ultsch M, Kossiakoff A. Human growth hormone and extracellular domain of its receptor: crystal structure of the complex. Science 1992;255:306-312.
    • (1992) Science , vol.255 , pp. 306-312
    • Vos, A.D.1    Ultsch, M.2    Kossiakoff, A.3
  • 68
    • 0001414449 scopus 로고    scopus 로고
    • Probing intermolecular main chain hydrogen bonding in serine proteinase-protein inhibitor complexes: Chemical synthesis of backbone-engineered turkey ovomucoid third domain
    • Lu WY, Qasim MA, Laskowski M, Kent SBH. Probing intermolecular main chain hydrogen bonding in serine proteinase-protein inhibitor complexes: chemical synthesis of backbone-engineered turkey ovomucoid third domain. Biochemistry 1997;36:673-679.
    • (1997) Biochemistry , vol.36 , pp. 673-679
    • Lu, W.Y.1    Qasim, M.A.2    Laskowski, M.3    Kent, S.B.H.4
  • 69
    • 0001289399 scopus 로고
    • Amino acid sequence homology between a serine protease inhibitor from barley Hordeum vulgare cultivar Hiproly and potato inhibitor I
    • Svendsen I, Jonassen I, Hejgaard J, Boisen S. Amino acid sequence homology between a serine protease inhibitor from barley Hordeum vulgare cultivar Hiproly and potato inhibitor I. Carsberg Res Commun 1980;45:389-395.
    • (1980) Carsberg Res Commun , vol.45 , pp. 389-395
    • Svendsen, I.1    Jonassen, I.2    Hejgaard, J.3    Boisen, S.4
  • 70
    • 0011704372 scopus 로고
    • A novel technique for the detection of dissociation-association equilibrium in highly associable macromolecular systems
    • Akasaka K, Fujii S, Hayashi F, Rokushika S, Hatano H. A novel technique for the detection of dissociation-association equilibrium in highly associable macromolecular systems. Biochem Int 1982;5: 637-642.
    • (1982) Biochem Int , vol.5 , pp. 637-642
    • Akasaka, K.1    Fujii, S.2    Hayashi, F.3    Rokushika, S.4    Hatano, H.5
  • 71
    • 0031024397 scopus 로고    scopus 로고
    • Interscaffolding additivity: Association of P-1 variants of eglin C and of turkey ovomucoid third domain with serine proteinases
    • Qasim MA, Ganz PJ, Saunders CW, Bateman KS, James MNG, Laskowski M. Interscaffolding additivity: association of P-1 variants of eglin C and of turkey ovomucoid third domain with serine proteinases. Biochemistry 1997;36:1598-1607.
    • (1997) Biochemistry , vol.36 , pp. 1598-1607
    • Qasim, M.A.1    Ganz, P.J.2    Saunders, C.W.3    Bateman, K.S.4    James, M.N.G.5    Laskowski, M.6
  • 72
    • 0032540358 scopus 로고    scopus 로고
    • Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity
    • Clackson T, Ultsch MH, Wells JA, deVos AM. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity. J Mol Biol 1998;277:1111-1128.
    • (1998) J Mol Biol , vol.277 , pp. 1111-1128
    • Clackson, T.1    Ultsch, M.H.2    Wells, J.A.3    DeVos, A.M.4
  • 73
    • 0027318108 scopus 로고
    • Directed mutagenesis and barnase-barstar recognition
    • Hartley RW. Directed mutagenesis and barnase-barstar recognition. Biochemistry 1993;32:5978-5984.
    • (1993) Biochemistry , vol.32 , pp. 5978-5984
    • Hartley, R.W.1
  • 74
    • 0028784163 scopus 로고
    • Two heads are better than one: Crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin
    • van deLocht A, Lamba D, Bauer M, Huber R, Friedrich T, Kroger B, Hoffken W, Bode W. Two heads are better than one: crystal structure of the insect derived double domain Kazal inhibitor rhodniin in complex with thrombin. EMBO J 1995;14:5149-5157.
    • (1995) EMBO J , vol.14 , pp. 5149-5157
    • Van DeLocht, A.1    Lamba, D.2    Bauer, M.3    Huber, R.4    Friedrich, T.5    Kroger, B.6    Hoffken, W.7    Bode, W.8
  • 75
    • 0029119320 scopus 로고
    • A preference-based free energy parameterization of enzyme-inhibitor binding applications to HIV-1 protease inhibitor design
    • Wallqvist A, Jernigan RL, Covell DG. A preference-based free energy parameterization of enzyme-inhibitor binding applications to HIV-1 protease inhibitor design. Protein Sci 1995;4:1881-1903.
    • (1995) Protein Sci , vol.4 , pp. 1881-1903
    • Wallqvist, A.1    Jernigan, R.L.2    Covell, D.G.3
  • 76
    • 0028911034 scopus 로고
    • A structural basis of the inacteractions between leucine-rich repeats and protein ligands
    • Kobe B, Deisenhofer J. A structural basis of the inacteractions between leucine-rich repeats and protein ligands. Nature 1995;374: 183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 77
    • 0015387337 scopus 로고
    • Trypsin-pancreatic inhibitor association: Dynamic of the interaction and role of disulfide bridges
    • Vincent JP, Lazdunski M. Trypsin-pancreatic inhibitor association: dynamic of the interaction and role of disulfide bridges. Biochemistry 1972;11:2967-2977.
    • (1972) Biochemistry , vol.11 , pp. 2967-2977
    • Vincent, J.P.1    Lazdunski, M.2
  • 78
    • 0036721253 scopus 로고    scopus 로고
    • Stability of macromolecular complexes
    • Brooijmans N, Sharp KA, Kuntz ID. Stability of macromolecular complexes. Proteins 2002;48:645-653.
    • (2002) Proteins , vol.48 , pp. 645-653
    • Brooijmans, N.1    Sharp, K.A.2    Kuntz, I.D.3


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