메뉴 건너뛰기




Volumn 6, Issue 10, 1997, Pages 2166-2179

Ligand binding to proteins: The binding landscape model

Author keywords

Global stability; HP lattice model; Hydrogen exchange; Ligand binding; Protein flexibility

Indexed keywords

ARTICLE; BINDING SITE; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STABILITY; PROTON TRANSPORT;

EID: 0030867610     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560061011     Document Type: Article
Times cited : (150)

References (51)
  • 3
    • 0025822867 scopus 로고
    • Solvent denaturation and stabilization of globular proteins
    • Alonso DOV, Dill KA. 1991. Solvent denaturation and stabilization of globular proteins. Biochemistry 30:5974-5985.
    • (1991) Biochemistry , vol.30 , pp. 5974-5985
    • Alonso, D.O.V.1    Dill, K.A.2
  • 5
    • 0026801082 scopus 로고
    • Long-range changes in a protein antigen due to antigen-antibody interaction
    • Benjamin DC, Williams DC, Smith-Gill SJ, Rule GS. 1992. Long-range changes in a protein antigen due to antigen-antibody interaction. Biochemistry 31:9539-9545.
    • (1992) Biochemistry , vol.31 , pp. 9539-9545
    • Benjamin, D.C.1    Williams, D.C.2    Smith-Gill, S.J.3    Rule, G.S.4
  • 6
    • 0028036120 scopus 로고
    • Multiple highly diverse structures complementary to enzyme binding sites: Results of extensive application of a de novo design method incorporating combinatorial growth
    • Bohacek RS, McMartin C. 1994. Multiple highly diverse structures complementary to enzyme binding sites: Results of extensive application of a de novo design method incorporating combinatorial growth. J Am Chem Soc 116:5560-5571.
    • (1994) J Am Chem Soc , vol.116 , pp. 5560-5571
    • Bohacek, R.S.1    McMartin, C.2
  • 8
    • 0025150383 scopus 로고
    • Origins of structure in globular proteins
    • Chan HS, Dill KA. 1990. Origins of structure in globular proteins. Proc Natl Acad Sci USA 87:6388-6392.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6388-6392
    • Chan, H.S.1    Dill, K.A.2
  • 9
    • 33744825406 scopus 로고
    • "Sequence space soup" of proteins and copolymers
    • Chan HS, Dill KA. 1991. "Sequence space soup" of proteins and copolymers. J Chem Phys 95:3775-3787.
    • (1991) J Chem Phys , vol.95 , pp. 3775-3787
    • Chan, H.S.1    Dill, K.A.2
  • 10
    • 36449000646 scopus 로고
    • Transition states and folding dynamics of proteins and heteropolymers
    • Chan HS, Dill KA. 1994. Transition states and folding dynamics of proteins and heteropolymers. J Chem Phys 100:9238-9257.
    • (1994) J Chem Phys , vol.100 , pp. 9238-9257
    • Chan, H.S.1    Dill, K.A.2
  • 13
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill KA. 1990. Dominant forces in protein folding. Biochemistry 29:7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 15
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill KA, Chan HS. 1997. From Levinthal to pathways to funnels. Nature Struct Biol 4:10-19.
    • (1997) Nature Struct Biol , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 16
    • 0020855355 scopus 로고
    • Structural dynamics of proteins and nucleic acids
    • Englander SW, Kallenbach NR. 1984. Structural dynamics of proteins and nucleic acids. Q Rev Biophys 16:521-655.
    • (1984) Q Rev Biophys , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 17
    • 0026320866 scopus 로고
    • The energy landscapes and motions of proteins
    • Frauenfelder H, Sligar SG, Wolynes PG. 1991. The energy landscapes and motions of proteins. Science 254:1598-1603.
    • (1991) Science , vol.254 , pp. 1598-1603
    • Frauenfelder, H.1    Sligar, S.G.2    Wolynes, P.G.3
  • 18
    • 0019872611 scopus 로고
    • Hydrogen exchange rates in pancreatic trypsin inhibitor are not correlated to thermal stability in urea
    • Hilton BD, Trudeau K, Woodward CK. 1981. Hydrogen exchange rates in pancreatic trypsin inhibitor are not correlated to thermal stability in urea. Biochemistry 20:4697-4703.
    • (1981) Biochemistry , vol.20 , pp. 4697-4703
    • Hilton, B.D.1    Trudeau, K.2    Woodward, C.K.3
  • 19
    • 0013994339 scopus 로고
    • Hydrogen exchange in proteins
    • Hvidt A, Nielsen SO. 1966. Hydrogen exchange in proteins. Adv Protein Chem 21:287-386.
    • (1966) Adv Protein Chem , vol.21 , pp. 287-386
    • Hvidt, A.1    Nielsen, S.O.2
  • 20
    • 0013863816 scopus 로고
    • Comparison of experimental binding data and theoretical models in proteins containing subunits
    • Koshland DE, Nemethy G, Filmer D. 1966. Comparison of experimental binding data and theoretical models in proteins containing subunits. Biochemistry 5:365-385.
    • (1966) Biochemistry , vol.5 , pp. 365-385
    • Koshland, D.E.1    Nemethy, G.2    Filmer, D.3
  • 21
    • 0020488766 scopus 로고
    • Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique
    • Kossiakoff AA. 1982. Protein dynamics investigated by the neutron diffraction-hydrogen exchange technique. Nature 296:713-721.
    • (1982) Nature , vol.296 , pp. 713-721
    • Kossiakoff, A.A.1
  • 22
    • 0029093363 scopus 로고
    • Local perturbations by ligand binding of hydrogen deuterium exchange kinetics in a four-helix bundle protein, acyl coenzyme A binding protein (ACBP)
    • Kragelund BB, Knudsen J, Poulsen FM. 1995. Local perturbations by ligand binding of hydrogen deuterium exchange kinetics in a four-helix bundle protein, acyl coenzyme A binding protein (ACBP). J Mol Biol 250:695-706.
    • (1995) J Mol Biol , vol.250 , pp. 695-706
    • Kragelund, B.B.1    Knudsen, J.2    Poulsen, F.M.3
  • 23
    • 0026730489 scopus 로고
    • Structure-based strategies for drug design and discovery
    • Kuntz ID. 1992. Structure-based strategies for drug design and discovery. Science 257:1078-1082.
    • (1992) Science , vol.257 , pp. 1078-1082
    • Kuntz, I.D.1
  • 24
    • 0024750637 scopus 로고
    • A lattice statistical mechanics model of the conformational and sequence spaces of proteins
    • Lau KF, Dill KA. 1989. A lattice statistical mechanics model of the conformational and sequence spaces of proteins. Macromolecules 22:3986-3997.
    • (1989) Macromolecules , vol.22 , pp. 3986-3997
    • Lau, K.F.1    Dill, K.A.2
  • 25
    • 0025101549 scopus 로고
    • Theory for protein mutability and biogenesis
    • Lau KF, Dill KA. 1990. Theory for protein mutability and biogenesis. Proc Natl Acad Sci USA 87:638-642.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 638-642
    • Lau, K.F.1    Dill, K.A.2
  • 26
    • 0019774669 scopus 로고
    • Molecular dynamics of hydrogen bonds in bovine pancreatic trypsin inhibitor protein
    • Levitt M. 1981. Molecular dynamics of hydrogen bonds in bovine pancreatic trypsin inhibitor protein. Nature 294:379-380.
    • (1981) Nature , vol.294 , pp. 379-380
    • Levitt, M.1
  • 27
    • 0027384196 scopus 로고
    • Hydrogen exchange in unligated and ligated staphylococcal nuclease
    • Loh SN, Prehoda KE, Wang J, Markley JL. 1993. Hydrogen exchange in unligated and ligated staphylococcal nuclease. Biochemistry 32:11022-11028.
    • (1993) Biochemistry , vol.32 , pp. 11022-11028
    • Loh, S.N.1    Prehoda, K.E.2    Wang, J.3    Markley, J.L.4
  • 28
    • 0001800583 scopus 로고
    • The mobile defect hypothesis of protein function
    • Lumry R, Rosenberg A. 1975. The mobile defect hypothesis of protein function. Colloq Int CNRS 246:55-63.
    • (1975) Colloq Int CNRS , vol.246 , pp. 55-63
    • Lumry, R.1    Rosenberg, A.2
  • 29
    • 0029868304 scopus 로고    scopus 로고
    • Locating and characterizing binding sites on proteins
    • Mattos C, Ringe D. 1996. Locating and characterizing binding sites on proteins. Nature Biotech 14:595-599.
    • (1996) Nature Biotech , vol.14 , pp. 595-599
    • Mattos, C.1    Ringe, D.2
  • 30
    • 0027520474 scopus 로고
    • Structure and dynamics of barnase complexed with 3′-GMP studied by NMR spectroscopy
    • Meiering EM, Bycroft M, Lubienski MJ, Fersht AR. 1993. Structure and dynamics of barnase complexed with 3′-GMP studied by NMR spectroscopy. Biochemistry 32:10975-10987.
    • (1993) Biochemistry , vol.32 , pp. 10975-10987
    • Meiering, E.M.1    Bycroft, M.2    Lubienski, M.J.3    Fersht, A.R.4
  • 31
    • 0029088938 scopus 로고
    • A statistical mechanical model for hydrogen exchange in globular proteins
    • Miller DW, Dill KA. 1995. A statistical mechanical model for hydrogen exchange in globular proteins. Protein Sci 4:1860-1873.
    • (1995) Protein Sci , vol.4 , pp. 1860-1873
    • Miller, D.W.1    Dill, K.A.2
  • 32
    • 78651189765 scopus 로고
    • On the nature of allosteric transitions: A plausible model
    • Monod J, Wyman J, Changeux JP. 1965. On the nature of allosteric transitions: A plausible model. J Mol Biol 12:88-118.
    • (1965) J Mol Biol , vol.12 , pp. 88-118
    • Monod, J.1    Wyman, J.2    Changeux, J.P.3
  • 33
    • 0029067489 scopus 로고
    • Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity
    • Morton A, Matthews BW. 1995. Specificity of ligand binding in a buried nonpolar cavity of T4 lysozyme: Linkage of dynamics and structural plasticity. Biochemistry 34:8576-8588.
    • (1995) Biochemistry , vol.34 , pp. 8576-8588
    • Morton, A.1    Matthews, B.W.2
  • 34
    • 0028236501 scopus 로고
    • Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B domain
    • Orban J, Alexander P, Bryan P. 1994. Hydrogen-deuterium exchange in the free and immunoglobulin G-bound protein G B domain. Biochemistry 33:5702-5710.
    • (1994) Biochemistry , vol.33 , pp. 5702-5710
    • Orban, J.1    Alexander, P.2    Bryan, P.3
  • 35
    • 0025142485 scopus 로고
    • An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR
    • Paterson Y, Englander SW, Roder H. 1990. An antibody binding site on cytochrome c defined by hydrogen exchange and two-dimensional NMR. Science 249:755-759.
    • (1990) Science , vol.249 , pp. 755-759
    • Paterson, Y.1    Englander, S.W.2    Roder, H.3
  • 36
    • 0002278852 scopus 로고
    • Packing defects, cavities, volume fluctuations, and access to the interior of proteins
    • Richards FM. 1979. Packing defects, cavities, volume fluctuations, and access to the interior of proteins. Carlsberg Res Commun 44:47-63.
    • (1979) Carlsberg Res Commun , vol.44 , pp. 47-63
    • Richards, F.M.1
  • 37
    • 0022399120 scopus 로고
    • Amide proton exchange in proteins by EX1 kinetics: Studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature
    • Roder H, Wagner G, Wuthrich K. 1985. Amide proton exchange in proteins by EX1 kinetics: Studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature. Biochemistry 24:7396-7407.
    • (1985) Biochemistry , vol.24 , pp. 7396-7407
    • Roder, H.1    Wagner, G.2    Wuthrich, K.3
  • 38
    • 0016699207 scopus 로고
    • Macromolecular binding
    • Schellman JA. 1975. Macromolecular binding. Biopolymers 14:999-1018.
    • (1975) Biopolymers , vol.14 , pp. 999-1018
    • Schellman, J.A.1
  • 39
    • 0014060322 scopus 로고
    • The tritium-hydrogen exchange of myosin and its proteolytic fragments
    • Segal DM, Harrington WF. 1967. The tritium-hydrogen exchange of myosin and its proteolytic fragments. Biochemistry 6:768-787.
    • (1967) Biochemistry , vol.6 , pp. 768-787
    • Segal, D.M.1    Harrington, W.F.2
  • 42
    • 0028286474 scopus 로고
    • Protein conformational change induced by 1, 1′-Bis (4-anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK
    • Shi L, Palleros DR, Fink AL. 1994. Protein conformational change induced by 1, 1′-Bis (4-anilino-5-naphthalenesulfonic acid): Preferential binding to the molten globule of DnaK. Biochemistry 33:7536-7546.
    • (1994) Biochemistry , vol.33 , pp. 7536-7546
    • Shi, L.1    Palleros, D.R.2    Fink, A.L.3
  • 44
    • 0027050824 scopus 로고
    • Modeling the effects of mutations on the denatured states of proteins
    • Shortle D, Chan HS, Dill KA. 1991. Modeling the effects of mutations on the denatured states of proteins. Protein Sci 1:201-215.
    • (1991) Protein Sci , vol.1 , pp. 201-215
    • Shortle, D.1    Chan, H.S.2    Dill, K.A.3
  • 46
    • 0027484016 scopus 로고
    • Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation
    • Thomas PD, Dill KA. 1993. Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation. Protein Sci 2:2050-2065.
    • (1993) Protein Sci , vol.2 , pp. 2050-2065
    • Thomas, P.D.1    Dill, K.A.2
  • 47
    • 0026696690 scopus 로고
    • Identification of a protein-binding surface by differential amide hydrogen-exchange measurements. Application to Bowman-Birk serine-protease inhibitor
    • Werner MH, Wemmer DE. 1992. Identification of a protein-binding surface by differential amide hydrogen-exchange measurements. Application to Bowman-Birk serine-protease inhibitor. J Mol Biol 225:873-889.
    • (1992) J Mol Biol , vol.225 , pp. 873-889
    • Werner, M.H.1    Wemmer, D.E.2
  • 48
    • 0004259377 scopus 로고
    • Hydrogen exchange in ribonuclease A: Neutron diffraction study
    • Wlodawer A, Sjolin L. 1982. Hydrogen exchange in ribonuclease A: Neutron diffraction study. Proc Natl Acad Sci USA 79:1418-1422.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 1418-1422
    • Wlodawer, A.1    Sjolin, L.2
  • 49
    • 0018368695 scopus 로고
    • Hydrogen exchange kinetics and internal motions in proteins and nucleic acids
    • Woodward CK, Hilton BD. 1979. Hydrogen exchange kinetics and internal motions in proteins and nucleic acids. Annu Rev Biophys Bioeng 8:99-127.
    • (1979) Annu Rev Biophys Bioeng , vol.8 , pp. 99-127
    • Woodward, C.K.1    Hilton, B.D.2
  • 50
    • 0015218157 scopus 로고
    • Studies of hydrogen exchange in proteins. VI. Urea effects on RNase hydrogen exchange kinetics leading to a general model for hydrogen exchange from folded proteins
    • Woodward CK, Rosenberg A. 1971. Studies of hydrogen exchange in proteins. VI. Urea effects on RNase hydrogen exchange kinetics leading to a general model for hydrogen exchange from folded proteins. J Biol Chem 246:4114-4121.
    • (1971) J Biol Chem , vol.246 , pp. 4114-4121
    • Woodward, C.K.1    Rosenberg, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.