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Volumn 50, Issue 14, 2011, Pages 2939-2950

A survey of aspartate-phenylalanine and glutamate-phenylalanine interactions in the protein data bank: Searching for anion-π pairs

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC RINGS; ASPARTATES; ENERGY CALCULATION; HIGH RESOLUTION; IN-SILICO; JACKSON; NON-COVALENT INTERACTION; PAIRWISE INTERACTION; POSITIVELY CHARGED; PROTEIN DATA BANK; PROTEIN STRUCTURES; QUADRUPOLE INTERACTIONS; REPULSIVE INTERACTION ENERGY; STABILIZING INTERACTIONS; STRUCTURAL STABILITIES;

EID: 79953701671     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi200066k     Document Type: Review
Times cited : (100)

References (88)
  • 2
    • 0035449064 scopus 로고    scopus 로고
    • More hydrogen bonds for the (structural) biologist
    • DOI 10.1016/S0968-0004(01)01935-1, PII S0968000401019351
    • Weiss, M. S., Brandl, M., Suhnel, J., Pal, D., and Hilgenfeld, R. (2001) More hydrogen bonds for the (structural) biologist Trends Biochem. Sci. 26, 521-523 (Pubitemid 32823428)
    • (2001) Trends in Biochemical Sciences , vol.26 , Issue.9 , pp. 521-523
    • Weiss, M.S.1    Brandl, M.2    Suhnel, J.3    Pal, D.4    Hilgenfeld, R.5
  • 3
    • 0037019829 scopus 로고    scopus 로고
    • CH·O hydrogen bonds at protein-protein interfaces
    • Jiang, L. and Lai, L. (2002) CH·O hydrogen bonds at protein-protein interfaces J. Biol. Chem. 277, 37732-37740
    • (2002) J. Biol. Chem. , vol.277 , pp. 37732-37740
    • Jiang, L.1    Lai, L.2
  • 4
    • 9944222091 scopus 로고    scopus 로고
    • δ-H·O=C hydrogen bonds involving proline residues in helices
    • δ-H·O=C hydrogen bonds involving proline residues in helices J. Phys. Chem. B 108, 18065-18072
    • (2004) J. Phys. Chem. B , vol.108 , pp. 18065-18072
    • Guo, H.1    Beahm, R.F.2    Guo, H.3
  • 6
    • 0030033588 scopus 로고    scopus 로고
    • Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp
    • Dougherty, D. A. (1996) Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp Science 271, 163-168 (Pubitemid 26033294)
    • (1996) Science , vol.271 , Issue.5246 , pp. 163-168
    • Dougherty, D.A.1
  • 9
    • 33749607747 scopus 로고    scopus 로고
    • High-accuracy quantum mechanical studies of π-π interactions in benzene dimers
    • DOI 10.1021/jp0610416
    • Sinnokrot, M. O. and Sherrill, C. D. (2006) High-accuracy quantum mechanical studies of π-π interactions in benzene dimers J. Phys. Chem. A 110, 10656-10668 (Pubitemid 44547206)
    • (2006) Journal of Physical Chemistry A , vol.110 , Issue.37 , pp. 10656-10668
    • Sinnokrot, M.O.1    Sherrill, C.D.2
  • 10
    • 33744470857 scopus 로고    scopus 로고
    • Benchmark database of accurate (MP2 and CCSD(T) complete basis set limit) interaction energies of small model complexes, DNA base pairs, and amino acid pairs
    • Jurecka, P., Sponer, J., Cerny, J., and Hobza, P. (2006) Benchmark database of accurate (MP2 and CCSD(T) complete basis set limit) interaction energies of small model complexes, DNA base pairs, and amino acid pairs Phys. Chem. Chem. Phys. 8, 1985-1993
    • (2006) Phys. Chem. Chem. Phys. , vol.8 , pp. 1985-1993
    • Jurecka, P.1    Sponer, J.2    Cerny, J.3    Hobza, P.4
  • 12
    • 34547529693 scopus 로고    scopus 로고
    • A preference for edgewise interactions between aromatic rings and carboxylate anions: The biological relevance of anion-quadrupole interactions
    • DOI 10.1021/jp0661995
    • Jackson, M. R., Beahm, R., Duvvuru, S., Narasimhan, C., Wu, J., Wang, H. N., Philip, V. M., Hinde, R. J., and Howell, E. E. (2007) A preference for edgewise interactions between aromatic rings and carboxylate anions: The biological relevance of anion-quadrupole interactions J. Phys. Chem. B 111, 8242-8249 (Pubitemid 47184400)
    • (2007) Journal of Physical Chemistry B , vol.111 , Issue.28 , pp. 8242-8249
    • Jackson, M.R.1    Beahm, R.2    Duvvuru, S.3    Narasimhan, C.4    Wu, J.5    Wang, H.-N.6    Philip, V.M.7    Hinde, R.J.8    Howell, E.E.9
  • 14
  • 16
    • 0033565007 scopus 로고    scopus 로고
    • Can lone pairs bind to a π system? the water·hexafluorobenzene interaction
    • Gallivan, J. P. and Dougherty, D. A. (1999) Can lone pairs bind to a π system? The water·hexafluorobenzene interaction Org. Lett. 1, 103-105
    • (1999) Org. Lett. , vol.1 , pp. 103-105
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 17
    • 0001291983 scopus 로고    scopus 로고
    • 6 and Electron-Donor Atoms
    • Alkorta, I., Rozas, I., and Elguero, J. (1997) An Attractive Interaction Between the π-Cloud of C6F6 and Electron-Donor Atoms J. Org. Chem. 62, 4687-4691 (Pubitemid 127494855)
    • (1997) Journal of Organic Chemistry , vol.62 , Issue.14 , pp. 4687-4691
    • Alkorta, I.1    Rozas, I.2    Elguero, J.3
  • 18
    • 84962408603 scopus 로고    scopus 로고
    • Anion-aromatic bonding: A case for anion recognition by π-acidic rings
    • DOI 10.1021/ja017449s
    • Mascal, M., Armstrong, A., and Bartberger, M. D. (2002) Anion-aromatic bonding: A case for anion recognition by π-acidic rings J. Am. Chem. Soc. 124, 6274-6276 (Pubitemid 34579378)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.22 , pp. 6274-6276
    • Mascal, M.1    Armstrong, A.2    Bartberger, M.D.3
  • 19
    • 1442311735 scopus 로고    scopus 로고
    • Theoretical Investigations of Anion-π Interactions: The Role of Anions and the Nature of π Systems
    • Kim, D., Tarakeshwar, P., and Kim, K. (2004) Theoretical Investigations of Anion-π Interactions: The Role of Anions and the Nature of π Systems J. Phys. Chem. A 108, 1250-1258
    • (2004) J. Phys. Chem. A , vol.108 , pp. 1250-1258
    • Kim, D.1    Tarakeshwar, P.2    Kim, K.3
  • 20
    • 0001120215 scopus 로고    scopus 로고
    • On the Nature of the Water-Hexafluorobenzene Interaction
    • Danten, Y., Tassaing, T., and Besnard, M. (1999) On the Nature of the Water-Hexafluorobenzene Interaction J. Phys. Chem. A 103, 3530-3534
    • (1999) J. Phys. Chem. A , vol.103 , pp. 3530-3534
    • Danten, Y.1    Tassaing, T.2    Besnard, M.3
  • 21
    • 8344248463 scopus 로고    scopus 로고
    • Cation-π versus anion-π interactions: Energetic, charge transfer and aromatic aspects
    • Garau, C., Frontera, A., Quinonero, D., Ballester, P., Costa, A., and Deya, P. (2004) Cation-π versus anion-π interactions: Energetic, charge transfer and aromatic aspects J. Phys. Chem. A 108, 9423-9427
    • (2004) J. Phys. Chem. A , vol.108 , pp. 9423-9427
    • Garau, C.1    Frontera, A.2    Quinonero, D.3    Ballester, P.4    Costa, A.5    Deya, P.6
  • 22
    • 20344381816 scopus 로고    scopus 로고
    • Structure and binding energy of anion-π and cation-π complexes: A comparison of MP2, RI-MP2, DFT, and DF-DFT methods
    • DOI 10.1021/jp044616c
    • Quinonero, D., Garau, C., Frontera, A., Ballester, P., Costa, A., and Deya, P. M. (2005) Structure and binding energy of anion-π and cation-π complexes; A comparison of MP2, RI-MP2, DFT and DF-DFT methods J. Phys. Chem. A 109, 4632-4637 (Pubitemid 40786045)
    • (2005) Journal of Physical Chemistry A , vol.109 , Issue.20 , pp. 4632-4637
    • Quinonero, D.1    Garau, C.2    Frontera, A.3    Ballester, P.4    Costa, A.5    Deya, P.M.6
  • 23
    • 10944227366 scopus 로고    scopus 로고
    • Cation-π vs anion-π interactions: A complete π-orbital analysis
    • DOI 10.1016/j.cplett.2004.10.014, PII S0009261404015805
    • Garau, C., Frontera, A., Quinonero, D., Ballester, P., Costa, A., and Deya, P. (2004) Cation-π vs anion-π interactions: A complete π-orbital analysis Chem. Phys. Lett. 399, 220-225 (Pubitemid 40017608)
    • (2004) Chemical Physics Letters , vol.399 , Issue.1-3 , pp. 220-225
    • Garau, C.1    Frontera, A.2    Quinonero, D.3    Ballester, P.4    Costa, A.5    Deya, P.M.6
  • 24
    • 2942701830 scopus 로고    scopus 로고
    • Cation-π versus anion-π interactions: A comparative ab initio study based on energetic, electron charge density and aromatic features
    • Garau, C., Frontera, A., Quinonero, D., Ballester, P., Costa, A., and Deya, P. M. (2004) Cation-π versus anion-π interactions: A comparative ab initio study based on energetic, electron charge density and aromatic features Chem. Phys. Lett. 392, 85-89
    • (2004) Chem. Phys. Lett. , vol.392 , pp. 85-89
    • Garau, C.1    Frontera, A.2    Quinonero, D.3    Ballester, P.4    Costa, A.5    Deya, P.M.6
  • 30
    • 33645454184 scopus 로고    scopus 로고
    • Anion-π interaction augments halide binding in solution
    • Berryman, O. B., Hof, F., Hynes, M. J., and Johnson, D. W. (2006) Anion-π interaction augments halide binding in solution Chem. Commun., 506-508
    • (2006) Chem. Commun. , pp. 506-508
    • Berryman, O.B.1    Hof, F.2    Hynes, M.J.3    Johnson, D.W.4
  • 31
    • 0020173901 scopus 로고
    • Electronic distributions within protein phenylalanine aromatic rings are reflected by the three-dimensional oxygen atom environments
    • Thomas, K. A., Smith, G. M., Thomas, T. B., and Feldmann, R. J. (1982) Electronic distributions within protein phenylalanine aromatic rings are reflected by the three-dimensional oxygen atom environments Proc. Natl. Acad. Sci. U.S.A. 79, 4843-4847
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 4843-4847
    • Thomas, K.A.1    Smith, G.M.2    Thomas, T.B.3    Feldmann, R.J.4
  • 32
    • 0024260626 scopus 로고
    • Weakly polar interactions in proteins
    • Burley, S. K. and Petsko, G. A. (1988) Weakly polar interactions in proteins Adv. Protein Chem. 39, 125-189
    • (1988) Adv. Protein Chem. , vol.39 , pp. 125-189
    • Burley, S.K.1    Petsko, G.A.2
  • 33
    • 0035841343 scopus 로고    scopus 로고
    • Characterization of aromatic-thiol π-type hydrogen bonding and phenylalanine-cysteine side chain interactions through ab initio calculations and protein database analyses
    • DOI 10.1080/00268970110063917
    • Duan, G., Smith, V. D., Jr., and Weaver, D. F. (2001) Characterization of aromatic-thiol π-type hydrogen bonding and phenylalanine-cysteine side chain interactions through ab initio calculations and protein database analyses Mol. Phys. 99, 1689-1699 (Pubitemid 35227786)
    • (2001) Molecular Physics , vol.99 , Issue.19 , pp. 1689-1699
    • Duan, G.1    Smith, V.H.2    Weaver, D.F.3
  • 34
    • 0242417008 scopus 로고    scopus 로고
    • Interactions with aromatic rings in chemical and biological recognition
    • DOI 10.1002/anie.200390319
    • Meyer, E. A., Castellano, R. K., and Diederich, F. (2003) Interactions with aromatic rings in chemical and biological recognition Angew. Chem., Int. Ed. 42, 1210-1250 (Pubitemid 36410287)
    • (2003) Angewandte Chemie - International Edition , vol.42 , Issue.11 , pp. 1210-1250
    • Meyer, E.A.1    Castellano, R.K.2    Diederich, F.3
  • 37
    • 0034812328 scopus 로고    scopus 로고
    • Polar interactions with aromatic side chains in α-helical peptides: Ch···O H-bonding and cation-π interactions
    • DOI 10.1021/ja015590v
    • Olson, C. A., Shi, Z., and Kallenbach, N. R. (2001) Polar interactions with aromatic side chains in α-helical peptides: CH·O H-bonding and cation-π interactions J. Am. Chem. Soc. 123, 6451-6452 (Pubitemid 32904687)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.26 , pp. 6451-6452
    • Olson, C.A.1    Shi, Z.2    Kallenbach, N.R.3
  • 38
    • 0037059067 scopus 로고    scopus 로고
    • Non-classical helix-stabilizing interactions: C-H·O H-bonding between Phe and Glu side chains in α-helical peptides
    • DOI 10.1016/S0301-4622(02)00171-0, PII S0301462202001710
    • Shi, Z., Olson, C. A., Bell, A. J., Jr., and Kallenbach, N. R. (2002) Non-classical helix-stabilizing interactions: C-H·O H-bonding between Phe and Glu side chains in α-helical peptides Biophys. Chem. 101-102, 267-279 (Pubitemid 35469128)
    • (2002) Biophysical Chemistry , vol.101-102 , pp. 267-279
    • Shi, Z.1    Olson, C.A.2    Bell Jr., A.J.3    Kallenbach, N.R.4
  • 39
    • 17744390877 scopus 로고    scopus 로고
    • Action-at-a-distance interactions enhance protein binding affinity
    • DOI 10.1110/ps.041283105
    • Joughin, B. A., Green, D. F., and Tidor, B. (2005) Action-at-a-distance interactions enhance protein binding affinity Protein Sci. 14, 1363-1369 (Pubitemid 40577816)
    • (2005) Protein Science , vol.14 , Issue.5 , pp. 1363-1369
    • Joughin, B.A.1    Green, D.F.2    Tidor, B.3
  • 41
    • 65749099472 scopus 로고    scopus 로고
    • The importance of being tyrosine: Lessons in molecular recognition from minimalist synthetic binding proteins
    • Koide, S. and Sidhu, S. S. (2009) The importance of being tyrosine: Lessons in molecular recognition from minimalist synthetic binding proteins Chem. Biol. 4, 325-334
    • (2009) Chem. Biol. , vol.4 , pp. 325-334
    • Koide, S.1    Sidhu, S.S.2
  • 42
    • 33644783935 scopus 로고    scopus 로고
    • Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code
    • DOI 10.1016/j.jmb.2005.11.092, PII S0022283605015597
    • Fellouse, F. A., Barthelemy, P. A., Kelley, R. F., and Sidhu, S. S. (2006) Tyrosine plays a dominant functional role in the paratope of a synthetic antibody derived from a four amino acid code J. Mol. Biol. 357, 100-114 (Pubitemid 43339317)
    • (2006) Journal of Molecular Biology , vol.357 , Issue.1 , pp. 100-114
    • Fellouse, F.A.1    Barthelemy, P.A.2    Kelley, R.F.3    Sidhu, S.S.4
  • 45
    • 67649631300 scopus 로고    scopus 로고
    • DevS Oxy Complex Stability Identifies This Heme Protein as a Gas Sensor in Mycobacterium tuberculosis Dormancy
    • Ioanoviciu, A., Meharenna, Y. T., Poulos, T. L., and Ortiz de Montellano, P. R. (2009) DevS Oxy Complex Stability Identifies This Heme Protein as a Gas Sensor in Mycobacterium tuberculosis Dormancy Biochemistry 48, 5839-5848
    • (2009) Biochemistry , vol.48 , pp. 5839-5848
    • Ioanoviciu, A.1    Meharenna, Y.T.2    Poulos, T.L.3    Ortiz De Montellano, P.R.4
  • 46
    • 65249108127 scopus 로고    scopus 로고
    • 2,1 Dihedral Angle-W3 Band Frequency Relationship to a Full Rotation: Correlations and Caveats
    • 2,1 Dihedral Angle-W3 Band Frequency Relationship to a Full Rotation: Correlations and Caveats Biochemistry 48, 2777-2787
    • (2009) Biochemistry , vol.48 , pp. 2777-2787
    • Juszczak, L.J.1    Desamero, R.Z.B.2
  • 47
    • 55949103773 scopus 로고    scopus 로고
    • Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion-quadrupole interaction with phosphoenolpyruvate carboxylate
    • Dharmarajan, L., Case, C. L., Dunten, P., and Mukhopadhyay, B. (2008) Tyr235 of human cytosolic phosphoenolpyruvate carboxykinase influences catalysis through an anion-quadrupole interaction with phosphoenolpyruvate carboxylate FEBS J. 275, 5810-5819
    • (2008) FEBS J. , vol.275 , pp. 5810-5819
    • Dharmarajan, L.1    Case, C.L.2    Dunten, P.3    Mukhopadhyay, B.4
  • 48
    • 0028972032 scopus 로고
    • NMR titrations with complexes between ds-DNA and indole derivatives including tryptophane containing peptides
    • Sartorius, J. and Schneider, H. J. (1995) NMR titrations with complexes between ds-DNA and indole derivatives including tryptophane containing peptides FEBS Lett. 374, 387-392
    • (1995) FEBS Lett. , vol.374 , pp. 387-392
    • Sartorius, J.1    Schneider, H.J.2
  • 49
    • 43449127780 scopus 로고    scopus 로고
    • Stacking interactions
    • Hobza, P. (2008) Stacking interactions Phys. Chem. Chem. Phys. 10, 2581-2583
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 2581-2583
    • Hobza, P.1
  • 50
    • 0028205447 scopus 로고
    • Enlarged representative set of protein structures
    • Hobohm, U. and Sander, C. (1994) Enlarged representative set of protein structures Protein Sci. 3, 522-524 (Pubitemid 24103723)
    • (1994) Protein Science , vol.3 , Issue.3 , pp. 522-524
    • Hobohm, U.1    Sander, C.2
  • 51
    • 0027092678 scopus 로고
    • Selection of representative protein data sets
    • Hobohm, U., Scharf, M., Schneider, R., and Sander, C. (1992) Selection of representative protein data sets Protein Sci. 1, 409-417 (Pubitemid 23007308)
    • (1992) Protein Science , vol.1 , Issue.3 , pp. 409-417
    • Hobohm, U.1    Scharf, M.2    Schneider, R.3    Sander, C.4
  • 53
    • 67649405075 scopus 로고    scopus 로고
    • Protein ionizable groups: PK values and their contribution to protein stability and solubility
    • Pace, C. N., Grimsley, G. R., and Scholtz, J. M. (2009) Protein ionizable groups: pK values and their contribution to protein stability and solubility J. Biol. Chem. 284, 13285-13289
    • (2009) J. Biol. Chem. , vol.284 , pp. 13285-13289
    • Pace, C.N.1    Grimsley, G.R.2    Scholtz, J.M.3
  • 57
    • 84987133653 scopus 로고
    • New energy decomposition scheme for molecular interactions within Hartree-Fock approximation
    • Kitaura, K. and Morokuma, K. (1976) New energy decomposition scheme for molecular interactions within Hartree-Fock approximation Int. J. Quantum Chem. 10, 325-340
    • (1976) Int. J. Quantum Chem. , vol.10 , pp. 325-340
    • Kitaura, K.1    Morokuma, K.2
  • 59
    • 0037025230 scopus 로고    scopus 로고
    • Cation-π interactions between ammonium ion and aromatic rings: An energy decomposition study
    • Aschi, M., Mazza, F., and Di Nola, A. (2002) Cation-π interactions between ammonium ion and aromatic rings: An energy decomposition study J. Mol. Struct. 587, 177-188
    • (2002) J. Mol. Struct. , vol.587 , pp. 177-188
    • Aschi, M.1    Mazza, F.2    Di Nola, A.3
  • 60
    • 33847088301 scopus 로고
    • The origin of hydrogen bonding. An energy decomposition study
    • Umeyama, H. and Morokuma, K. (1977) The origin of hydrogen bonding. An energy decomposition study J. Am. Chem. Soc. 99, 1316-1332
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 1316-1332
    • Umeyama, H.1    Morokuma, K.2
  • 61
    • 33746614482 scopus 로고
    • Gaussian basis sets for use in correlated molecular calculations. I. The atoms boron through neon and hydrogen
    • Dunning, T. H., Jr. (1989) Gaussian basis sets for use in correlated molecular calculations. I. The atoms boron through neon and hydrogen J. Chem. Phys. 90, 1007-1023
    • (1989) J. Chem. Phys. , vol.90 , pp. 1007-1023
    • Dunning Jr., T.H.1
  • 62
    • 4143095330 scopus 로고
    • Electron affinities of the first-row atoms revisited. Systematic basis sets and wave functions
    • Kendall, R. A., Dunning, T. H., Jr., and Harrison, R. J. (1992) Electron affinities of the first-row atoms revisited. Systematic basis sets and wave functions J. Chem. Phys. 96, 6796-6806
    • (1992) J. Chem. Phys. , vol.96 , pp. 6796-6806
    • Kendall, R.A.1    Dunning Jr., T.H.2    Harrison, R.J.3
  • 63
    • 84890021933 scopus 로고
    • The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors
    • Boys, S. and Bernardi, F. (1970) The calculation of small molecular interactions by the differences of separate total energies. Some procedures with reduced errors Mol. Phys. 19, 553-566
    • (1970) Mol. Phys. , vol.19 , pp. 553-566
    • Boys, S.1    Bernardi, F.2
  • 65
    • 79953682697 scopus 로고
    • Department of Chemistry, University of Arizona, Tucson, AZ (modified by J. Gosper at Brunel University, Uxbridge, West London, U.K.).
    • Walters, P. and Stahl, M. (1994) BABELwin, Department of Chemistry, University of Arizona, Tucson, AZ (modified by J. Gosper at Brunel University, Uxbridge, West London, U.K.) (ftp://joplin.biosci.arizona.edu/pub/Babel/).
    • (1994) BABELwin
    • Walters, P.1    Stahl, M.2
  • 66
    • 0015967881 scopus 로고
    • Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins
    • Chou, P. Y. and Fasman, G. D. (1974) Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteins Biochemistry 13, 211-222
    • (1974) Biochemistry , vol.13 , pp. 211-222
    • Chou, P.Y.1    Fasman, G.D.2
  • 67
    • 0015987426 scopus 로고
    • Prediction of protein conformation
    • Chou, P. Y. and Fasman, G. D. (1974) Prediction of protein conformation Biochemistry 13, 222-245
    • (1974) Biochemistry , vol.13 , pp. 222-245
    • Chou, P.Y.1    Fasman, G.D.2
  • 68
    • 0036081125 scopus 로고    scopus 로고
    • Factors contributing to decreased protein stability when aspartic acid residues are in β-sheet regions
    • DOI 10.1110/ps.4920102
    • Pokkuluri, P. R., Gu, M., Cai, X., Raffen, R., Stevens, F. J., and Schiffer, M. (2002) Factors contributing to decreased protein stability when aspartic acid residues are in β-sheet regions Protein Sci. 11, 1687-1694 (Pubitemid 34663548)
    • (2002) Protein Science , vol.11 , Issue.7 , pp. 1687-1694
    • Pokkuluri, P.R.1    Gu, M.2    Cai, X.3    Raffen, R.4    Stevens, F.J.5    Schiffer, M.6
  • 69
    • 0346614603 scopus 로고    scopus 로고
    • Multiple regression analysis of the beta-sheet propensity of amino acids
    • PII S0166128097001887
    • Niwa, T. S. and Ogino, A. (1997) Multiple regression analysis of the β-sheet propensity of amino acids THEOCHEM 419, 155-160 (Pubitemid 127437832)
    • (1997) Journal of Molecular Structure: THEOCHEM , vol.419 , Issue.1-3 , pp. 155-160
    • Niwa, T.S.1    Ogino, A.2
  • 70
    • 0001117058 scopus 로고    scopus 로고
    • Construction and design of β-sheets
    • Smith, C. K. and Regan, L. (1997) Construction and design of β-sheets Acc. Chem. Res. 30, 153-161
    • (1997) Acc. Chem. Res. , vol.30 , pp. 153-161
    • Smith, C.K.1    Regan, L.2
  • 72
    • 0036328545 scopus 로고    scopus 로고
    • CX, an algorithm that identifies protruding atoms in proteins
    • Pintar, A., Carugo, O., and Pongor, S. (2002) CX, an algorithm that identifies protruding atoms in proteins Bioinformatics 18, 980-984 (Pubitemid 34846481)
    • (2002) Bioinformatics , vol.18 , Issue.7 , pp. 980-984
    • Pintar, A.1    Carugo, O.2    Pongor, S.3
  • 75
    • 17144379313 scopus 로고    scopus 로고
    • Influence of the water molecule on cation-π interaction: Ab initio second order møller-plesset perturbation theory (MP2) calculations
    • DOI 10.1021/jp044568w
    • Xu, Y., Shen, J., Zhu, W., Luo, X., Chen, K., and Jiang, H. (2005) Influence of the Water Molecule on Cation-π Interaction: Ab Initio Second Order Muoler-Plesset Perturbation Theory (MP2) Calculations J. Phys. Chem. B 109, 5945-5949 (Pubitemid 40519504)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.12 , pp. 5945-5949
    • Xu, Y.1    Shen, J.2    Zhu, W.3    Luo, X.4    Chen, K.5    Jiang, H.6
  • 76
    • 33845575030 scopus 로고    scopus 로고
    • Contribution of cation-π interactions to protein stability
    • DOI 10.1021/bi061275f
    • Prajapati, R. S., Sirajuddin, M., Durani, V., Sreeramulu, S., and Varadarajan, R. (2006) Contribution of Cation-π Interactions to Protein Stability Biochemistry 45, 15000-15010 (Pubitemid 44937012)
    • (2006) Biochemistry , vol.45 , Issue.50 , pp. 15000-15010
    • Prajapati, R.S.1    Sirajuddin, M.2    Durani, V.3    Sreeramulu, S.4    Varadarajan, R.5
  • 77
    • 77149124231 scopus 로고    scopus 로고
    • Experimental and computational study of the interplay between C-H/π and anion-π interactions
    • Quinonero, D., Deya, P. M., Carranza, M. P., Rodriquex, A. M., Jalon, F. A., and Manzano, B. R. (2010) Experimental and computational study of the interplay between C-H/π and anion-π interactions Dalton Trans. 39, 794-806
    • (2010) Dalton Trans. , vol.39 , pp. 794-806
    • Quinonero, D.1    Deya, P.M.2    Carranza, M.P.3    Rodriquex, A.M.4    Jalon, F.A.5    Manzano, B.R.6
  • 78
    • 69949139295 scopus 로고    scopus 로고
    • Very long-range effects: Cooperativity between anion-π and hydrogen-bonding interactions
    • Lucas, X., Estarellas, C., Escudero, D., Frontera, A., Quinonero, D., and Deya, P. M. (2009) Very long-range effects: Cooperativity between anion-π and hydrogen-bonding interactions ChemPhysChem 10, 2256-2264
    • (2009) ChemPhysChem , vol.10 , pp. 2256-2264
    • Lucas, X.1    Estarellas, C.2    Escudero, D.3    Frontera, A.4    Quinonero, D.5    Deya, P.M.6
  • 81
    • 33646236303 scopus 로고    scopus 로고
    • Development of novel statistical potentials describing cation-π interactions in proteins and comparison with semiempirical and quantum chemistry approaches
    • Gilis, D., Biot, C., Buisine, E., Dehouck, Y., and Rooman, M. (2006) Development of novel statistical potentials describing cation-π interactions in proteins and comparison with semiempirical and quantum chemistry approaches J. Chem. Inf. Model. 46, 884-893
    • (2006) J. Chem. Inf. Model. , vol.46 , pp. 884-893
    • Gilis, D.1    Biot, C.2    Buisine, E.3    Dehouck, Y.4    Rooman, M.5
  • 83
    • 0000571928 scopus 로고    scopus 로고
    • Structural and topological aspects of anion coordination
    • Bianchi, A., Bowman-James, K., and Garcia-Espana, E., Eds.) pp - 215, Wiley-VCH, New York.
    • Atwood, J. and Steed, J. (1997) Structural and topological aspects of anion coordination. In Supramolecular Chemistry of Anions (Bianchi, A., Bowman-James, K., and Garcia-Espana, E., Eds.) pp 147 - 215, Wiley-VCH, New York.
    • (1997) Supramolecular Chemistry of Anions , pp. 147-225
    • Atwood, J.1    Steed, J.2
  • 85
    • 0031891022 scopus 로고    scopus 로고
    • Computation of electrostatic complements to proteins: A case of charge stabilized binding
    • Chong, L. T., Dempster, S. E., Hendsch, Z. S., Lee, L. P., and Tidor, B. (1998) Computation of electrostatic complements to proteins: A case of charge stabilized binding Protein Sci. 7, 206-210 (Pubitemid 28133762)
    • (1998) Protein Science , vol.7 , Issue.1 , pp. 206-210
    • Chong, L.T.1    Dempster, S.E.2    Hendsch, Z.S.3    Lee, L.-P.4    Tidor, B.5
  • 87
    • 70449529413 scopus 로고    scopus 로고
    • Molecular modeling and dynamics studies with explicit inclusion of electronic polarizability. Theory and applications
    • Lopes, P. E. M., Roux, B., and MacKerell, A. D., Jr. (2009) Molecular modeling and dynamics studies with explicit inclusion of electronic polarizability. Theory and applications Theor. Chem. Acc. 124, 11-28
    • (2009) Theor. Chem. Acc. , vol.124 , pp. 11-28
    • Lopes, P.E.M.1    Roux, B.2    Mackerell Jr., A.D.3
  • 88
    • 74249119329 scopus 로고    scopus 로고
    • Critical assessment of methods of protein structure prediction - Round VIII
    • Moult, J., Fidelis, K., Kryshtafovych, A., Rost, B., and Tramontano, A. (2009) Critical assessment of methods of protein structure prediction - Round VIII Proteins 77 (Suppl. 9) 1-4
    • (2009) Proteins , vol.77 , Issue.SUPPL. 9 , pp. 1-4
    • Moult, J.1    Fidelis, K.2    Kryshtafovych, A.3    Rost, B.4    Tramontano, A.5


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