메뉴 건너뛰기




Volumn 9, Issue 11, 2002, Pages 1209-1217

Analysis of the π-π stacking interactions between the aminoglycoside antibiotic kinase APH(3′)-IIIa and its nucleotide ligands

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; ADENOSINE DIPHOSPHATE; KANAMYCIN KINASE; LIGAND; TYROSINE;

EID: 0036851016     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(02)00245-4     Document Type: Article
Times cited : (90)

References (72)
  • 1
    • 0011164114 scopus 로고    scopus 로고
    • Noncovalent interactions: A challenge for experiment and theory
    • Müller-Dethlefs K., Hobza P. Noncovalent interactions. a challenge for experiment and theory Chem. Rev. 100:2000;143-167.
    • (2000) Chem. Rev. , vol.100 , pp. 143-167
    • Müller-Dethlefs, K.1    Hobza, P.2
  • 2
    • 0022419375 scopus 로고
    • Aromatic-aromatic interaction: A mechanism of protein structure stabilization
    • Burley S.K., Petsko G.A. Aromatic-aromatic interaction. a mechanism of protein structure stabilization Science. 229:1985;23-28.
    • (1985) Science , vol.229 , pp. 23-28
    • Burley, S.K.1    Petsko, G.A.2
  • 3
    • 0034678016 scopus 로고    scopus 로고
    • Mimicking the structure and function of DNA: Insights into DNA stability and replication
    • Kool E.T., Morales J.C., Guckian K.M. Mimicking the structure and function of DNA. insights into DNA stability and replication Angew. Chem. Int. Ed. Engl. 39:2000;990-1009.
    • (2000) Angew. Chem. Int. Ed. Engl. , vol.39 , pp. 990-1009
    • Kool, E.T.1    Morales, J.C.2    Guckian, K.M.3
  • 4
    • 0025878347 scopus 로고
    • π-π interactions: The geometry and energetics of phenylalanine-phenylalanine interactions in proteins
    • Hunter C.A., Singh J., Thornton J.M. π-π interactions. the geometry and energetics of phenylalanine-phenylalanine interactions in proteins J. Mol. Biol. 218:1991;837-846.
    • (1991) J. Mol. Biol. , vol.218 , pp. 837-846
    • Hunter, C.A.1    Singh, J.2    Thornton, J.M.3
  • 6
    • 0025756736 scopus 로고
    • Aromatic-aromatic interactions and protein stability
    • Serrano L., Bycroft M., Fersht A.R. Aromatic-aromatic interactions and protein stability. J. Mol. Biol. 218:1991;465-475.
    • (1991) J. Mol. Biol. , vol.218 , pp. 465-475
    • Serrano, L.1    Bycroft, M.2    Fersht, A.R.3
  • 7
    • 0032546782 scopus 로고    scopus 로고
    • π-stacking interactions: Alive and well in proteins
    • McGaughey G.B., Gagne M., Rappé A.K. π-stacking interactions. alive and well in proteins J. Biol. Chem. 271:1998;15458-15463.
    • (1998) J. Biol. Chem. , vol.271 , pp. 15458-15463
    • McGaughey, G.B.1    Gagne, M.2    Rappé, A.K.3
  • 8
    • 0032560940 scopus 로고    scopus 로고
    • NMR study of intramolecular interactions between aromatic groups: Van der waals, charge-transfer, or quadrupolar interactions?
    • Heaton N.J., Bello P., Herradón B., del Campo A., Jiménez-Barbero J. NMR study of intramolecular interactions between aromatic groups. van der waals, charge-transfer, or quadrupolar interactions? J. Am. Chem. Soc. 120:1998;9632-9645.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9632-9645
    • Heaton, N.J.1    Bello, P.2    Herradón, B.3    Del Campo, A.4    Jiménez-Barbero, J.5
  • 9
    • 0033601293 scopus 로고    scopus 로고
    • The structural basis for the increased immunogenicity of two HIV-reverse transcriptase peptide variant/class I major histocompatibility complexes
    • Kirksey T.J., Pogue-Caley R.R., Frelinger J.A., Collins E.J. The structural basis for the increased immunogenicity of two HIV-reverse transcriptase peptide variant/class I major histocompatibility complexes. J. Biol. Chem. 274:1999;37259-37264.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37259-37264
    • Kirksey, T.J.1    Pogue-Caley, R.R.2    Frelinger, J.A.3    Collins, E.J.4
  • 10
    • 0033578010 scopus 로고    scopus 로고
    • Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins
    • Ohndorf U.-M., Rould M.A., He Q., Pabo C.O., Lippard S.J. Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins. Nature. 299:1999;708-712.
    • (1999) Nature , vol.299 , pp. 708-712
    • Ohndorf, U.-M.1    Rould, M.A.2    He, Q.3    Pabo, C.O.4    Lippard, S.J.5
  • 11
    • 0031213649 scopus 로고    scopus 로고
    • The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions
    • Valegard K., Murray J.B., Stonehouse N.J., van den Worm S., Stockley P.G., Liljas L. The three-dimensional structures of two complexes between recombinant MS2 capsids and RNA operator fragments reveal sequence-specific protein-RNA interactions. J. Mol. Biol. 270:1997;724-738.
    • (1997) J. Mol. Biol. , vol.270 , pp. 724-738
    • Valegard, K.1    Murray, J.B.2    Stonehouse, N.J.3    Van den Worm, S.4    Stockley, P.G.5    Liljas, L.6
  • 12
    • 0028004607 scopus 로고
    • Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin
    • Oubridge C., Ito N., Evans P., Teo C.-H., Nagal K. Crystal structure at 1.92 Å resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin. Nature. 372:1994;432-438.
    • (1994) Nature , vol.372 , pp. 432-438
    • Oubridge, C.1    Ito, N.2    Evans, P.3    Teo, C.-H.4    Nagal, K.5
  • 13
    • 0032514483 scopus 로고    scopus 로고
    • Crystal structure of the spliceosomal U2B″-U2A′ protein complex bound to a fragment of U2 small nuclear RNA
    • Price S.R., Evans P.R., Nagal K. Crystal structure of the spliceosomal U2B″-U2A′ protein complex bound to a fragment of U2 small nuclear RNA. Nature. 394:1998;645-650.
    • (1998) Nature , vol.394 , pp. 645-650
    • Price, S.R.1    Evans, P.R.2    Nagal, K.3
  • 15
    • 0033615310 scopus 로고    scopus 로고
    • Recognition of an essential adenine at a protein-RNA interface: Comparison of the contributions of hydrogen bonds and a stacking arrangement
    • Nolan S.J., Shiels J.C., Tuite J.B., Cecere K.L., Baranger A.M. Recognition of an essential adenine at a protein-RNA interface. comparison of the contributions of hydrogen bonds and a stacking arrangement J. Am. Chem. Soc. 121:1999;8951-8952.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 8951-8952
    • Nolan, S.J.1    Shiels, J.C.2    Tuite, J.B.3    Cecere, K.L.4    Baranger, A.M.5
  • 18
    • 0030830868 scopus 로고    scopus 로고
    • Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases
    • Hon W.-C., McKay G.A., Thompson P.R., Sweet R.M., Yang D.S.C., Wright G.D., Berghuis A.M. Structure of an enzyme required for aminoglycoside antibiotic resistance reveals homology to eukaryotic protein kinases. Cell. 89:1997;887-895.
    • (1997) Cell , vol.89 , pp. 887-895
    • Hon, W.-C.1    McKay, G.A.2    Thompson, P.R.3    Sweet, R.M.4    Yang, D.S.C.5    Wright, G.D.6    Berghuis, A.M.7
  • 19
    • 0032570289 scopus 로고    scopus 로고
    • Structure-based redesign of corepressor specificity of the escherichia coli purine repressor by substitution of residue 190
    • Lu F., Schumacher M.A., Arvidson D.N., Haldimann A., Wanner B.L., Zalkin H., Brennan R.G. Structure-based redesign of corepressor specificity of the escherichia coli purine repressor by substitution of residue 190. Biochemistry. 37:1998;971-982.
    • (1998) Biochemistry , vol.37 , pp. 971-982
    • Lu, F.1    Schumacher, M.A.2    Arvidson, D.N.3    Haldimann, A.4    Wanner, B.L.5    Zalkin, H.6    Brennan, R.G.7
  • 20
    • 0029938467 scopus 로고    scopus 로고
    • Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7
    • Subramanya H.S., Doherty A.J., Ashford S.R., Wigley D.B. Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell. 85:1996;607-615.
    • (1996) Cell , vol.85 , pp. 607-615
    • Subramanya, H.S.1    Doherty, A.J.2    Ashford, S.R.3    Wigley, D.B.4
  • 22
    • 0029032663 scopus 로고
    • Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins
    • Huang Q., Liu S., Tang Y., Jin S., Wang Y. Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins. Biochem. J. 309:1995;285-298.
    • (1995) Biochem. J. , vol.309 , pp. 285-298
    • Huang, Q.1    Liu, S.2    Tang, Y.3    Jin, S.4    Wang, Y.5
  • 23
    • 0037129933 scopus 로고    scopus 로고
    • The "cap-binding slot" of an mRNA cap-binding protein: Quantitative effects of aromatic side chain choice in the double-stacking sandwich with cap
    • Hu G., Oguro A., Li C., Gershon P.D., Quiocho F.A. The "cap-binding slot" of an mRNA cap-binding protein. quantitative effects of aromatic side chain choice in the double-stacking sandwich with cap Biochemistry. 41:2002;7677-7678.
    • (2002) Biochemistry , vol.41 , pp. 7677-7678
    • Hu, G.1    Oguro, A.2    Li, C.3    Gershon, P.D.4    Quiocho, F.A.5
  • 24
    • 0029151201 scopus 로고
    • CH/π interaction in the packing of the adenine ring in protein structures
    • Chakrabarti P., Uttamkumar S. CH/π interaction in the packing of the adenine ring in protein structures. J. Mol. Biol. 251:1995;9-14.
    • (1995) J. Mol. Biol. , vol.251 , pp. 9-14
    • Chakrabarti, P.1    Uttamkumar, S.2
  • 25
    • 0035979336 scopus 로고    scopus 로고
    • Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase
    • Burk D.L., Hon W.C., Leung A.K.-W., Berghuis A.M. Structural analyses of nucleotide binding to an aminoglycoside phosphotransferase. Biochemistry. 40:2001;8756-8764.
    • (2001) Biochemistry , vol.40 , pp. 8756-8764
    • Burk, D.L.1    Hon, W.C.2    Leung, A.K.-W.3    Berghuis, A.M.4
  • 26
    • 0028358078 scopus 로고
    • Broad spectrum aminoglycoside phosphotransferase type III from enterococcus: Overexpression, purification, and substrate specificity
    • McKay G.A., Thompson P.R., Wright G.D. Broad spectrum aminoglycoside phosphotransferase type III from enterococcus. overexpression, purification, and substrate specificity Biochemistry. 33:1994;6936-6944.
    • (1994) Biochemistry , vol.33 , pp. 6936-6944
    • McKay, G.A.1    Thompson, P.R.2    Wright, G.D.3
  • 27
    • 0029941909 scopus 로고    scopus 로고
    • Catalytic mechanism of enterococcal kanamycin kinase (APH(3′)-IIIa): Viscosity, thio, and solvent isotope effects support a Theorell-Chance mechanism
    • McKay G.A., Wright G.D. Catalytic mechanism of enterococcal kanamycin kinase (APH(3′)-IIIa). viscosity, thio, and solvent isotope effects support a Theorell-Chance mechanism Biochemistry. 35:1996;8680-8685.
    • (1996) Biochemistry , vol.35 , pp. 8680-8685
    • McKay, G.A.1    Wright, G.D.2
  • 28
    • 0034940585 scopus 로고    scopus 로고
    • Aminoglycoside-modifying enzymes: Mechanisms of catalytic processes and inhibition
    • Azucena E., Mobashery S. Aminoglycoside-modifying enzymes. mechanisms of catalytic processes and inhibition Drug Resist. Updat. 4:2001;106-117.
    • (2001) Drug Resist. Updat. , vol.4 , pp. 106-117
    • Azucena, E.1    Mobashery, S.2
  • 29
    • 0032226544 scopus 로고    scopus 로고
    • Aminoglycoside antibiotics: Structures, functions and resistance
    • Wright G.D., Berghuis A.M., Mobashery S. Aminoglycoside antibiotics. structures, functions and resistance Adv. Exp. Med. Biol. 456:1998;27-69.
    • (1998) Adv. Exp. Med. Biol. , vol.456 , pp. 27-69
    • Wright, G.D.1    Berghuis, A.M.2    Mobashery, S.3
  • 30
    • 0036237683 scopus 로고    scopus 로고
    • Aminoglycoside modified by resistance enzymes display diminished binding to the bacterial ribosomal aminoacyl-tRNA site
    • Llano-Sotelo B., Azucena E., Kotra L.P., Mobashery S., Chow C.S. Aminoglycoside modified by resistance enzymes display diminished binding to the bacterial ribosomal aminoacyl-tRNA site. Chem. Biol. 9:2002;455-463.
    • (2002) Chem. Biol. , vol.9 , pp. 455-463
    • Llano-Sotelo, B.1    Azucena, E.2    Kotra, L.P.3    Mobashery, S.4    Chow, C.S.5
  • 31
    • 0034123845 scopus 로고    scopus 로고
    • Resisting resistance: New chemical strategies for battling superbugs
    • Wright G.D. Resisting resistance. new chemical strategies for battling superbugs Chem. Biol. 7:2000;R127-R132.
    • (2000) Chem. Biol. , vol.7
    • Wright, G.D.1
  • 32
    • 0032774575 scopus 로고    scopus 로고
    • Aminoglycoside antibiotic phosphotransferases are also serine protein kinases
    • Daigle D.M., McKay G.A., Thompson P.R., Wright G.D. Aminoglycoside antibiotic phosphotransferases are also serine protein kinases. Chem. Biol. 6:1999;11-18.
    • (1999) Chem. Biol. , vol.6 , pp. 11-18
    • Daigle, D.M.1    McKay, G.A.2    Thompson, P.R.3    Wright, G.D.4
  • 33
    • 0035968312 scopus 로고    scopus 로고
    • Molecular mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa: Roles of conserved active site residues
    • Boehr D.D., Thompson P.R., Wright G.D. Molecular mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa. roles of conserved active site residues J. Biol. Chem. 276:2001;23929-23936.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23929-23936
    • Boehr, D.D.1    Thompson, P.R.2    Wright, G.D.3
  • 34
    • 0037018922 scopus 로고    scopus 로고
    • Mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa: Role of the nucleotide positioning loop
    • Thompson P.R., Boehr D.D., Berghuis A.M., Wright G.D. Mechanism of aminoglycoside antibiotic kinase APH(3′)-IIIa. role of the nucleotide positioning loop Biochemistry. 41:2002;7001-7007.
    • (2002) Biochemistry , vol.41 , pp. 7001-7007
    • Thompson, P.R.1    Boehr, D.D.2    Berghuis, A.M.3    Wright, G.D.4
  • 35
    • 0034602208 scopus 로고    scopus 로고
    • Tethered bisubstrate derivatives as probes for mechanism and as inhibitors of aminoglycoside 3′-phosphotransferases
    • Liu M., Haddad J., Azucena E., Kotra L.P., Kirzhner M., Mobashery S. Tethered bisubstrate derivatives as probes for mechanism and as inhibitors of aminoglycoside 3′-phosphotransferases. J. Org. Chem. 65:2000;7422-7431.
    • (2000) J. Org. Chem. , vol.65 , pp. 7422-7431
    • Liu, M.1    Haddad, J.2    Azucena, E.3    Kotra, L.P.4    Kirzhner, M.5    Mobashery, S.6
  • 36
    • 0028879950 scopus 로고
    • Loss of individual electrostatic interactions between aminoglycoside antibiotics and resistance enzymes as an effective means to overcoming bacterial drug resistance
    • Roestamadji J., Graspas I., Mobashery S. Loss of individual electrostatic interactions between aminoglycoside antibiotics and resistance enzymes as an effective means to overcoming bacterial drug resistance. J. Am. Chem. Soc. 117:1995;11060-11069.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 11060-11069
    • Roestamadji, J.1    Graspas, I.2    Mobashery, S.3
  • 37
    • 0032534816 scopus 로고    scopus 로고
    • The use of neamine as a molecular template: Inactivation of bacterial antibiotic resistance enzyme aminoglycoside 3′-phosphotransferase type IIa
    • Roestamadji J., Mobashery S. The use of neamine as a molecular template. inactivation of bacterial antibiotic resistance enzyme aminoglycoside 3′-phosphotransferase type IIa Bioorg. Med. Chem. Lett. 8:1998;3483-3488.
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 3483-3488
    • Roestamadji, J.1    Mobashery, S.2
  • 39
    • 0034872155 scopus 로고    scopus 로고
    • Active site labeling of the gentamicin resistance enzyme AAC(6′)-APH(2″) by the lipid kinase inhibitor wortmannin
    • Boehr D.D., Lane W.S., Wright G.D. Active site labeling of the gentamicin resistance enzyme AAC(6′)-APH(2″) by the lipid kinase inhibitor wortmannin. Chem. Biol. 8:2001;791-800.
    • (2001) Chem. Biol. , vol.8 , pp. 791-800
    • Boehr, D.D.1    Lane, W.S.2    Wright, G.D.3
  • 40
    • 0030848695 scopus 로고    scopus 로고
    • Inhibition of aminoglycoside antibiotic resistance enzymes by protein kinase inhibitors
    • Daigle D.M., McKay G.A., Wright G.D. Inhibition of aminoglycoside antibiotic resistance enzymes by protein kinase inhibitors. J. Biol. Chem. 272:1997;24755-24758.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24755-24758
    • Daigle, D.M.1    McKay, G.A.2    Wright, G.D.3
  • 41
    • 0014440879 scopus 로고
    • Quantum-mechanical investigations of the electronic structure of nucleic acids and their constituents
    • Pullman B., Pullman A. Quantum-mechanical investigations of the electronic structure of nucleic acids and their constituents. Prog. Nucleic Acid Res. Mol. Biol. 9:1969;327-403.
    • (1969) Prog. Nucleic Acid Res. Mol. Biol. , vol.9 , pp. 327-403
    • Pullman, B.1    Pullman, A.2
  • 42
    • 0029745052 scopus 로고    scopus 로고
    • Cation-π interactions in aromatics of biological interest: Electrostatic potential surfaces as a useful qualitative guide
    • Mecozzi S., West A.P., Dougherty D.A. Cation-π interactions in aromatics of biological interest. electrostatic potential surfaces as a useful qualitative guide Proc. Natl. Acad. Sci. USA. 93:1996;10566-10571.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10566-10571
    • Mecozzi, S.1    West, A.P.2    Dougherty, D.A.3
  • 44
    • 0028882693 scopus 로고
    • Kinetic mechanism of aminoglycoside phosphotransferase type IIIa: Evidence for a Theorell-Chance mechanism
    • McKay G.A., Wright G.D. Kinetic mechanism of aminoglycoside phosphotransferase type IIIa. evidence for a Theorell-Chance mechanism J. Biol. Chem. 270:1995;24686-24692.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24686-24692
    • McKay, G.A.1    Wright, G.D.2
  • 45
    • 0025370815 scopus 로고
    • Dominant forces in protein folding
    • Dill K.A. Dominant forces in protein folding. Biochemistry. 29:1990;7133-7155.
    • (1990) Biochemistry , vol.29 , pp. 7133-7155
    • Dill, K.A.1
  • 46
    • 0027478123 scopus 로고
    • Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes
    • Shaw K.J., Rather P.N., Hare R.S., Miller G.H. Molecular genetics of aminoglycoside resistance genes and familial relationships of the aminoglycoside-modifying enzymes. Microbiol. Rev. 57:1993;138-163.
    • (1993) Microbiol. Rev. , vol.57 , pp. 138-163
    • Shaw, K.J.1    Rather, P.N.2    Hare, R.S.3    Miller, G.H.4
  • 47
    • 0034837523 scopus 로고    scopus 로고
    • Molecular dynamics and thermodynamics of protein-RNA interactions: Mutation of a conserved aromatic residue modifies stacking interactions and structural adaptation in the U1A-stem loop 2 RNA complex
    • Blakaj D.M., McConnell K.J., Beveridge D.L., Baranger A.M. Molecular dynamics and thermodynamics of protein-RNA interactions. mutation of a conserved aromatic residue modifies stacking interactions and structural adaptation in the U1A-stem loop 2 RNA complex J. Am. Chem. Soc. 123:2001;2548-2551.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 2548-2551
    • Blakaj, D.M.1    McConnell, K.J.2    Beveridge, D.L.3    Baranger, A.M.4
  • 48
    • 0030454007 scopus 로고    scopus 로고
    • Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex
    • LeCuyer K.A., Behlen L.S., Uhlenbeck O.C. Mutagenesis of a stacking contact in the MS2 coat protein-RNA complex. EMBO J. 15:1996;6847-6853.
    • (1996) EMBO J. , vol.15 , pp. 6847-6853
    • LeCuyer, K.A.1    Behlen, L.S.2    Uhlenbeck, O.C.3
  • 49
    • 0033618268 scopus 로고    scopus 로고
    • Thermodynamics of unpaired terminal nucleotides on short RNA helixes correlates with stacking at helix termini in larger RNAs
    • Burkard M.E., Kierzek R., Turner D.H. Thermodynamics of unpaired terminal nucleotides on short RNA helixes correlates with stacking at helix termini in larger RNAs. J. Mol. Biol. 290:1999;967-982.
    • (1999) J. Mol. Biol. , vol.290 , pp. 967-982
    • Burkard, M.E.1    Kierzek, R.2    Turner, D.H.3
  • 50
    • 0029118487 scopus 로고
    • A free energy analysis of nucleic acid base stacking in aqueous solution
    • Friedman R.A., Honig B. A free energy analysis of nucleic acid base stacking in aqueous solution. Biophys. J. 69:1995;1528-1535.
    • (1995) Biophys. J. , vol.69 , pp. 1528-1535
    • Friedman, R.A.1    Honig, B.2
  • 51
    • 0030001537 scopus 로고    scopus 로고
    • Benzene dimer: A good model for π-π interactions in proteins? A comparison between the benzene and the toluene dimers in the gas phase and in an aqueous solution
    • Chipot C., Jaffe R., Maigret B., Pearlman D.A., Kollman P.A. Benzene dimer. a good model for π-π interactions in proteins? A comparison between the benzene and the toluene dimers in the gas phase and in an aqueous solution J. Am. Chem. Soc. 118:1996;11217-11224.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 11217-11224
    • Chipot, C.1    Jaffe, R.2    Maigret, B.3    Pearlman, D.A.4    Kollman, P.A.5
  • 52
    • 0037045235 scopus 로고    scopus 로고
    • Origin of the attraction and directionality of the π/π interaction: Model chemistry calculations of benzene dimer interaction
    • Tsuzuki S., Honda K., Uchimaru T., Mikami M., Tanabe K. Origin of the attraction and directionality of the π/π interaction. model chemistry calculations of benzene dimer interaction J. Am. Chem. Soc. 124:2002;104-112.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 104-112
    • Tsuzuki, S.1    Honda, K.2    Uchimaru, T.3    Mikami, M.4    Tanabe, K.5
  • 53
  • 54
    • 0001543861 scopus 로고
    • Aromatic stacking interactions in aqueous solution: Evidence that neither classical hydrophobic effects nor dispersion forces are important
    • Newcomb L.F., Gellman S.H. Aromatic stacking interactions in aqueous solution. evidence that neither classical hydrophobic effects nor dispersion forces are important J. Am. Chem. Soc. 116:1994;4993-4994.
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 4993-4994
    • Newcomb, L.F.1    Gellman, S.H.2
  • 55
    • 0030345452 scopus 로고    scopus 로고
    • New evidence that the hydrophobic effect and dispersion are not major driving forces for nucleotide base stacking
    • Gellman S.H., Haque T.S., Newcomb L.F. New evidence that the hydrophobic effect and dispersion are not major driving forces for nucleotide base stacking. Biophys. J. 71:1996;3523-3526.
    • (1996) Biophys. J. , vol.71 , pp. 3523-3526
    • Gellman, S.H.1    Haque, T.S.2    Newcomb, L.F.3
  • 56
    • 0035857392 scopus 로고    scopus 로고
    • Beyond the hydrophobic effect: Attractions involving heteroaromatic rings in aqueous solution
    • McKay S.L., Haptonstall B., Gellman S.H. Beyond the hydrophobic effect. attractions involving heteroaromatic rings in aqueous solution J. Am. Chem. Soc. 123:2001;1244-1245.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1244-1245
    • McKay, S.L.1    Haptonstall, B.2    Gellman, S.H.3
  • 57
    • 3643140670 scopus 로고
    • The electrostatic interactions in van der Waals complexes involving aromatic molecules
    • Price S.L., Stone A.J. The electrostatic interactions in van der Waals complexes involving aromatic molecules. J. Chem. Phys. 86:1987;2859-2868.
    • (1987) J. Chem. Phys. , vol.86 , pp. 2859-2868
    • Price, S.L.1    Stone, A.J.2
  • 58
    • 0000965687 scopus 로고    scopus 로고
    • Structure, energetics and dynamics of the nucleic acid base bairs: Nonempirical ab initio calculations
    • Hobza P., Sponer J. Structure, energetics and dynamics of the nucleic acid base bairs. nonempirical ab initio calculations Chem. Rev. 99:1999;3247-3276.
    • (1999) Chem. Rev. , vol.99 , pp. 3247-3276
    • Hobza, P.1    Sponer, J.2
  • 60
    • 0033518870 scopus 로고    scopus 로고
    • Computational and experimental studies of (2,2)-bis(indol-1-yl-methyl)acetate suggest the importance of the hydrophobic effect in aromatic stacking interactions
    • Pang Y.-P., Miller J.L., Kollman P.A. Computational and experimental studies of (2,2)-bis(indol-1-yl-methyl)acetate suggest the importance of the hydrophobic effect in aromatic stacking interactions. J. Am. Chem. Soc. 121:1999;1717-1725.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 1717-1725
    • Pang, Y.-P.1    Miller, J.L.2    Kollman, P.A.3
  • 61
    • 0032696761 scopus 로고    scopus 로고
    • Derivatives of n-benzyl-2-phenylpyridinium bromide, minimalist models for face-to-face, center-to-edge π stacking in water
    • Martin C.B., Mulla H.R., Willis P.G., Cammers-Goodwin A. Derivatives of n-benzyl-2-phenylpyridinium bromide, minimalist models for face-to-face, center-to-edge π stacking in water. J. Org. Chem. 64:1999;7802-7806.
    • (1999) J. Org. Chem. , vol.64 , pp. 7802-7806
    • Martin, C.B.1    Mulla, H.R.2    Willis, P.G.3    Cammers-Goodwin, A.4
  • 63
    • 0032522196 scopus 로고    scopus 로고
    • Influence of solvent on aromatic interactions in metal tris-bipyridine complexes
    • Breault G.A., Hunter C.A., Mayers P.C. Influence of solvent on aromatic interactions in metal tris-bipyridine complexes. J. Am. Chem. Soc. 120:1998;3402-3410.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 3402-3410
    • Breault, G.A.1    Hunter, C.A.2    Mayers, P.C.3
  • 64
    • 0037028989 scopus 로고    scopus 로고
    • Unexpected substituent effects in offset π-π stacked interactions in water
    • Rashkin M., Waters M.L. Unexpected substituent effects in offset π-π stacked interactions in water. J. Am. Chem. Soc. 124:2002;1860-1861.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1860-1861
    • Rashkin, M.1    Waters, M.L.2
  • 65
    • 0032483756 scopus 로고    scopus 로고
    • Measurements of molecular electrostatic field effects in edge-to-face aromatic interactions and CH-π interactions with implications for protein folding and molecular recognition
    • Kim E., Paliwal S., Wilcox C.S. Measurements of molecular electrostatic field effects in edge-to-face aromatic interactions and CH-π interactions with implications for protein folding and molecular recognition. J. Am. Chem. Soc. 120:1998;11192-11193.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11192-11193
    • Kim, E.1    Paliwal, S.2    Wilcox, C.S.3
  • 66
    • 84985553175 scopus 로고
    • Electron donor-acceptor interactions in host-guest complexes in organic solvents
    • Ferguson S.B., Diederich F. Electron donor-acceptor interactions in host-guest complexes in organic solvents. Angew. Chem. Int. Ed. 25:1986;1127-1129.
    • (1986) Angew. Chem. Int. Ed. , vol.25 , pp. 1127-1129
    • Ferguson, S.B.1    Diederich, F.2
  • 67
    • 0037140752 scopus 로고    scopus 로고
    • Stacking and T-shape competition in aromatic-aromatic amino acid interactions
    • Chelli R., Gervasio F.L., Procacci P., Schettino V. Stacking and T-shape competition in aromatic-aromatic amino acid interactions. J. Am. Chem. Soc. 124:2002;6133-6134.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6133-6134
    • Chelli, R.1    Gervasio, F.L.2    Procacci, P.3    Schettino, V.4
  • 70
    • 0036470051 scopus 로고    scopus 로고
    • Protein explorer: Easy yet powerful macromolecular visualization
    • Martz E. Protein explorer. easy yet powerful macromolecular visualization Trends Biochem. Sci. 27:2002;107-109.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 107-109
    • Martz, E.1
  • 71
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T., Williston S., Brandts J., Lin L.-N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179:1989;131-137.
    • (1989) Anal. Biochem. , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.3    Lin, L.-N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.