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Volumn 51, Issue 11, 2012, Pages 2309-2318

Weak interactions between folate and osmolytes in solution

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROFOLATE; DIHYDROFOLATE REDUCTASE; IN-VIVO; MODEL COMPOUND; NUCLEAR OVERHAUSER EFFECTS; OSMOLYTES; OSMOTIC STRESS; P-AMINOBENZOIC ACID; PREFERENTIAL INTERACTION; SMALL MOLECULES; SPECIFIC BINDING; SURFACE AREA; WEAK INTERACTIONS;

EID: 84858626900     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3000947     Document Type: Article
Times cited : (20)

References (50)
  • 1
    • 0032589204 scopus 로고    scopus 로고
    • Folate and vitamin B12
    • Scott, J. M. (1999) Folate and vitamin B12 Proc. Nutr. Soc. 58, 441-448
    • (1999) Proc. Nutr. Soc. , vol.58 , pp. 441-448
    • Scott, J.M.1
  • 2
    • 21044452600 scopus 로고    scopus 로고
    • Searching sequence space: Two different approaches to dihydrofolate reductase catalysis
    • DOI 10.1002/cbic.200400237
    • Howell, E. E. (2005) Searching sequence space: Two different approaches to dihydrofolate reductase catalysis ChemBioChem 6, 590-600 (Pubitemid 40873755)
    • (2005) ChemBioChem , vol.6 , Issue.4 , pp. 590-600
    • Howell, E.E.1
  • 4
    • 0023668190 scopus 로고
    • Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli
    • Fierke, C. A., Johnson, K. A., and Benkovic, S. J. (1987) Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli Biochemistry 26, 4085-4092
    • (1987) Biochemistry , vol.26 , pp. 4085-4092
    • Fierke, C.A.1    Johnson, K.A.2    Benkovic, S.J.3
  • 5
    • 0028800949 scopus 로고
    • A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site
    • Narayana, N., Matthews, D. A., Howell, E. E., and Nguyen-huu, X. (1995) A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site Nat. Struct. Biol. 2, 1018-1025
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1018-1025
    • Narayana, N.1    Matthews, D.A.2    Howell, E.E.3    Nguyen-Huu, X.4
  • 6
    • 0017262305 scopus 로고
    • The purification and properties of the trimethoprim-resistant dihydrofolate reductase mediated by the R-factor, R 388
    • Amyes, S. G. B. and Smith, J. T. (1976) The purification and properties of the trimethoprim-resistant dihydrofolate reductase mediated by the R-factor, R 388 Eur. J. Biochem. 61, 597-603
    • (1976) Eur. J. Biochem. , vol.61 , pp. 597-603
    • Amyes, S.G.B.1    Smith, J.T.2
  • 7
    • 41949105752 scopus 로고    scopus 로고
    • A balancing act: Net uptake of water during dihydrofolate binding and net release of water upon NADPH binding in R67 dihydrofolate reductase
    • Chopra, S., Dooling, R., Horner, C. G., and Howell, E. E. (2008) A balancing act: Net uptake of water during dihydrofolate binding and net release of water upon NADPH binding in R67 dihydrofolate reductase J. Biol. Chem. 283, 4690-4698
    • (2008) J. Biol. Chem. , vol.283 , pp. 4690-4698
    • Chopra, S.1    Dooling, R.2    Horner, C.G.3    Howell, E.E.4
  • 8
    • 79955586889 scopus 로고    scopus 로고
    • Thermodynamics and solvent effects on substrate and cofactor binding in Esherichia coli chromosomal dihydrofolate reductase
    • Grubbs, J., Rahmanian, S., DeLuca, A., Padmashali, C., Jackson, M., Duff, M. R., Jr., and Howell, E. E. (2011) Thermodynamics and solvent effects on substrate and cofactor binding in Esherichia coli chromosomal dihydrofolate reductase Biochemistry 50, 3673-3685
    • (2011) Biochemistry , vol.50 , pp. 3673-3685
    • Grubbs, J.1    Rahmanian, S.2    Deluca, A.3    Padmashali, C.4    Jackson, M.5    Duff Jr., M.R.6    Howell, E.E.7
  • 9
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa, T. and Timasheff, S. N. (1985) The stabilization of proteins by osmolytes Biophys. J. 47, 411-414
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 10
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff, S. N. (1993) The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 22, 67-97 (Pubitemid 23180317)
    • (1993) Annual Review of Biophysics and Biomolecular Structure , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 12
    • 36949079198 scopus 로고
    • Crystalline dihydropteroylglutamic acid
    • Blakley, R. L. (1960) Crystalline dihydropteroylglutamic acid Nature 188, 231-232
    • (1960) Nature , vol.188 , pp. 231-232
    • Blakley, R.L.1
  • 13
    • 0015860668 scopus 로고
    • Proton magnetic resonance studies of folate, dihydrofolate, and methotrexate. Evidence from pH and concentration studies for dimerization
    • Poe, M. (1973) Proton magnetic resonance studies of folate, dihydrofolate, and methotrexate. Evidence from pH and concentration studies for dimerization J. Biol. Chem. 248, 7025-7032
    • (1973) J. Biol. Chem. , vol.248 , pp. 7025-7032
    • Poe, M.1
  • 14
    • 0020345697 scopus 로고
    • Buffers of constant ionic strength for studying pH-dependent processes
    • Ellis, K. J. and Morrison, J. F. (1982) Buffers of constant ionic strength for studying pH-dependent processes Methods Enzymol. 87, 405-426
    • (1982) Methods Enzymol. , vol.87 , pp. 405-426
    • Ellis, K.J.1    Morrison, J.F.2
  • 15
    • 0026750592 scopus 로고
    • Human dihydrofolate reductase: Reduction of alternative substrates, pH effects, and inhibition by deazafolates
    • Williams, E. A. and Morrison, J. F. (1992) Human dihydrofolate reductase: Reduction of alternative substrates, pH effects, and inhibition by deazafolates Biochemistry 31, 6801-6811
    • (1992) Biochemistry , vol.31 , pp. 6801-6811
    • Williams, E.A.1    Morrison, J.F.2
  • 16
    • 84855909168 scopus 로고    scopus 로고
    • MestRe Nova
    • Willcott, M. R. (2009) MestRe Nova J. Am. Chem. Soc. 131, 13180-13180
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13180-13180
    • Willcott, M.R.1
  • 17
    • 13944258032 scopus 로고    scopus 로고
    • Solutes probe hydration in specific association of cyclodextrin and adamantane
    • DOI 10.1021/ja045541t
    • Harries, D., Rau, D. C., and Parsegian, V. A. (2005) Solutes probe hydration in specific association of cyclodextrin and adamantane J. Am. Chem. Soc. 127, 2184-2190 (Pubitemid 40270522)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.7 , pp. 2184-2190
    • Harries, D.1    Rau, D.C.2    Parsegian, V.A.3
  • 19
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • DOI 10.1016/0003-2697(89)90213-3
    • Wiseman, T., Williston, S., Brandts, J. F., and Lin, L. N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179, 131-137 (Pubitemid 19149635)
    • (1989) Analytical Biochemistry , vol.179 , Issue.1 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.-N.4
  • 20
    • 33845937672 scopus 로고    scopus 로고
    • Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: Application to adaptor protein complexes in cell signaling
    • DOI 10.1110/ps.062558507
    • Houtman, J. C., Brown, P. H., Bowden, B., Yamaguchi, H., Appella, E., Samelson, L. E., and Schuck, P. (2007) Studying multisite binary and ternary protein interactions by global analysis of isothermal titration calorimetry data in SEDPHAT: Application to adaptor protein complexes in cell signaling Protein Sci. 16, 30-42 (Pubitemid 46036496)
    • (2007) Protein Science , vol.16 , Issue.1 , pp. 30-42
    • Houtman, J.C.D.1    Brown, P.H.2    Bowden, B.3    Yamaguchi, H.4    Appella, E.5    Samelson, L.E.6    Schuck, P.7
  • 22
    • 0017735327 scopus 로고
    • Acidic dissociation constants of folic acid, dihydrofolic acid, and methotrexate
    • Poe, M. (1977) Acidic dissociation constants of folic acid, dihydrofolic acid, and methotrexate J. Biol. Chem. 252, 3724-3728 (Pubitemid 8116108)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.11 , pp. 3724-3728
    • Poe, M.1
  • 23
    • 33748943839 scopus 로고    scopus 로고
    • Determination of dissociation constants of folic acid, methotrexate, and other photolabile pteridines by pressure-assisted capillary electrophoresis
    • DOI 10.1002/elps.200600128
    • Szakacs, Z. and Noszal, B. (2006) Determination of dissociation constants of folic acid, methotrexate, and other photolabile pteridines by pressure-assisted capillary electrophoresis Electrophoresis 27, 3399-3409 (Pubitemid 44430720)
    • (2006) Electrophoresis , vol.27 , Issue.17 , pp. 3399-3409
    • Szakacs, Z.1    Noszal, B.2
  • 26
    • 84858670926 scopus 로고
    • Solution conformation and intramolecular association of the pyridine Coenzymes
    • In (Everse, J. Anderson, B. and You, K.-S. Eds.) pp, Academic Press, New York
    • Oppenheimer, N. J. (1982) Solution conformation and intramolecular association of the pyridine Coenzymes. In The Pyridine Nucleotide Coenzymes (Everse, J., Anderson, B., and You, K.-S., Eds.) pp 68-89, Academic Press, New York.
    • (1982) The Pyridine Nucleotide Coenzymes , pp. 68-89
    • Oppenheimer, N.J.1
  • 29
    • 0026664548 scopus 로고
    • Atomic structure and chemistry of human serum albumin
    • He, X. M. and Carter, D. C. (1992) Atomic structure and chemistry of human serum albumin Nature 358, 209-215
    • (1992) Nature , vol.358 , pp. 209-215
    • He, X.M.1    Carter, D.C.2
  • 30
    • 0017891061 scopus 로고
    • The weak binding reaction between folate and human serum proteins
    • Zettner, A. and Duly, P. E. (1978) The weak binding reaction between folate and human serum proteins Ann. Clin. Lab. Sci. 8, 57-63 (Pubitemid 8272355)
    • (1978) Annals of Clinical and Laboratory Science , vol.8 , Issue.1 , pp. 57-63
    • Zettner, A.1    Duly, P.E.2
  • 31
    • 0027819337 scopus 로고
    • Hypersensitivity of an enzyme reaction to solvent water
    • DOI 10.1021/bi00086a020
    • Dzingeleski, G. D. and Wolfenden, R. (1993) Hypersensitivity of an enzyme reaction to solvent water Biochemistry 32, 9143-9147 (Pubitemid 24186236)
    • (1993) Biochemistry , vol.32 , Issue.35 , pp. 9143-9147
    • Dzingeleski, G.D.1    Wolfenden, R.2
  • 32
    • 0035918265 scopus 로고    scopus 로고
    • The role of water molecules in the association of cytochrome P450cam with putidaredoxin. An osmotic pressure study
    • Furukawa, Y. and Morishima, I. (2001) The role of water molecules in the association of cytochrome P450cam with putidaredoxin. An osmotic pressure study J. Biol. Chem. 276, 12983-12990
    • (2001) J. Biol. Chem. , vol.276 , pp. 12983-12990
    • Furukawa, Y.1    Morishima, I.2
  • 33
    • 0030770571 scopus 로고    scopus 로고
    • Involvement of water molecules in the association of monoclonal antibody HyHEL-5 with bobwhite quail lysozyme
    • Xavier, K. A., Shick, K. A., Smith-Gil, S. J., and Willson, R. C. (1997) Involvement of water molecules in the association of monoclonal antibody HyHEL-5 with bobwhite quail lysozyme Biophys. J. 73, 2116-2125 (Pubitemid 27425742)
    • (1997) Biophysical Journal , vol.73 , Issue.4 , pp. 2116-2125
    • Xavier, K.A.1    Shick, K.A.2    Smith-Gill, S.J.3    Willson, R.C.4
  • 34
    • 70350120306 scopus 로고    scopus 로고
    • Characterization of solvatomorphs of methotrexate using thermoanalytical and other techniques
    • Chadha, R., Arora, P., Kaur, R., Saini, A., Singla, M. L., and Jain, D. S. (2009) Characterization of solvatomorphs of methotrexate using thermoanalytical and other techniques Acta Pharm. (Zagreb, Croatia) 59, 245-257
    • (2009) Acta Pharm. (Zagreb, Croatia) , vol.59 , pp. 245-257
    • Chadha, R.1    Arora, P.2    Kaur, R.3    Saini, A.4    Singla, M.L.5    Jain, D.S.6
  • 35
    • 59649118049 scopus 로고    scopus 로고
    • Complexation of anthracene with folic acid studied by FTIR and UV spectroscopies
    • He, Y. Y., Wang, X. C., Jin, P. K., Zhao, B., and Fan, X. (2009) Complexation of anthracene with folic acid studied by FTIR and UV spectroscopies Spectrochim. Acta, Part A 72, 876-879
    • (2009) Spectrochim. Acta, Part A , vol.72 , pp. 876-879
    • He, Y.Y.1    Wang, X.C.2    Jin, P.K.3    Zhao, B.4    Fan, X.5
  • 36
    • 80054717093 scopus 로고    scopus 로고
    • Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer
    • Guinn, E. J., Pegram, L. M., Capp, M. W., Pollock, M. N., and Record, M. T., Jr. (2011) Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizer Proc. Natl. Acad. Sci. U.S.A. 108, 16932-16937
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 16932-16937
    • Guinn, E.J.1    Pegram, L.M.2    Capp, M.W.3    Pollock, M.N.4    Record Jr., M.T.5
  • 37
    • 70350513011 scopus 로고    scopus 로고
    • Interactions of the osmolyte glycine betaine with molecular surfaces in water: Thermodynamics, structural interpretation, and prediction of m-values
    • Capp, M. W., Pegram, L. M., Saecker, R. M., Kratz, M., Riccardi, D., Wendorff, T., Cannon, J. G., and Record, M. T., Jr. (2009) Interactions of the osmolyte glycine betaine with molecular surfaces in water: Thermodynamics, structural interpretation, and prediction of m-values Biochemistry 48, 10372-10379
    • (2009) Biochemistry , vol.48 , pp. 10372-10379
    • Capp, M.W.1    Pegram, L.M.2    Saecker, R.M.3    Kratz, M.4    Riccardi, D.5    Wendorff, T.6    Cannon, J.G.7    Record Jr., M.T.8
  • 38
    • 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
  • 39
    • 16544384573 scopus 로고    scopus 로고
    • The pH-dependence of preferential solvation as studied by intermolecular homo- and heteronuclear NOE measurements of adenosine in water-trifluoroethanol mixtures
    • DOI 10.1007/s00216-003-2308-0
    • Angulo, M. and Berger, S. (2004) The pH-dependence of preferential solvation as studied by intermolecular homo- and heteronuclear NOE measurements of adenosine in water-trifluoroethanol mixtures Anal. Bioanal. Chem. 378, 1555-1560 (Pubitemid 40877686)
    • (2004) Analytical and Bioanalytical Chemistry , vol.378 , Issue.6 , pp. 1555-1560
    • Angulo, M.1    Berger, S.2
  • 40
    • 0042821626 scopus 로고    scopus 로고
    • Site-specific solvation determined by intermolecular nuclear overhauser effect: Measurments and molecular dynamics
    • Angulo, M., Christoph, H., Hofmann, H.-J., and Berger, S. (2003) Site-specific solvation determined by intermolecular nuclear overhauser effect: Measurments and molecular dynamics Org. Biomol. Chem. 1, 1049-1052
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 1049-1052
    • Angulo, M.1    Christoph, H.2    Hofmann, H.-J.3    Berger, S.4
  • 41
    • 0018412079 scopus 로고
    • Role of serum folate binders in the delivery of folate to tissues and to the fetus
    • Fernandes-Costa, F. and Metz, J. (1979) Role of serum folate binders in the delivery of folate to tissues and to the fetus Br. J. Haematol. 41, 335-342 (Pubitemid 9109597)
    • (1979) British Journal of Haematology , vol.41 , Issue.3 , pp. 335-342
    • Fernandes-Costa, F.1    Metz, J.2
  • 42
    • 0018195047 scopus 로고
    • Specific and non-specific folate binding protein in normal and malignant human tissues
    • Corrocher, R., De Sandre, G., Ambrosetti, A., Pachor, M., Bambara, L., and Hoffbrand, A. (1978) Specific and non-specific folate binding protein in normal and malignant human tissues J. Clin. Pathol. 31, 659-665 (Pubitemid 8379772)
    • (1978) Journal of Clinical Pathology , vol.31 , Issue.7 , pp. 659-665
    • Corrocher, R.1    De Sandre, G.2    Ambrosetti, A.3
  • 43
    • 0022420273 scopus 로고
    • Guanine nucleotides modulate the ligand binding properties of cell surface folate receptors in Dictyostelium discoideum
    • De Wit, R. and Bulgakov, R. (1985) Guanine nucleotides modulate the ligand binding properties of cell surface folate receptors in Dictyostelium discoideum FEBS Lett. 179, 257-261
    • (1985) FEBS Lett. , vol.179 , pp. 257-261
    • De Wit, R.1    Bulgakov, R.2
  • 44
    • 0023008886 scopus 로고
    • The interaction of folylpolyglutamates with deoxyhemoglobin. Identification of the binding site
    • Arnone, A., Rogers, P. H., Benesch, R. E., Benesch, R., and Kwong, S. (1986) The interaction of folylpolyglutamates with deoxyhemoglobin. Identification of the binding site J. Biol. Chem. 261, 5853-5857
    • (1986) J. Biol. Chem. , vol.261 , pp. 5853-5857
    • Arnone, A.1    Rogers, P.H.2    Benesch, R.E.3    Benesch, R.4    Kwong, S.5
  • 45
    • 84856814983 scopus 로고    scopus 로고
    • Revealing the allosterome: Systematic identification of metabolite-protein interactions
    • Orsak, T., Smith, T. L., Eckert, D., Lindsley, J. E., Borges, C. R., and Rutter, J. (2012) Revealing the allosterome: Systematic identification of metabolite-protein interactions Biochemistry 51, 225-232
    • (2012) Biochemistry , vol.51 , pp. 225-232
    • Orsak, T.1    Smith, T.L.2    Eckert, D.3    Lindsley, J.E.4    Borges, C.R.5    Rutter, J.6
  • 46
    • 77955707910 scopus 로고    scopus 로고
    • Volume exclusion and soft interaction effects on protein stability under crowded conditions
    • Miklos, A. C., Li, C., Sharaf, N. G., and Pielak, G. J. (2010) Volume exclusion and soft interaction effects on protein stability under crowded conditions Biochemistry 49, 6984-6991
    • (2010) Biochemistry , vol.49 , pp. 6984-6991
    • Miklos, A.C.1    Li, C.2    Sharaf, N.G.3    Pielak, G.J.4
  • 47
    • 80055013471 scopus 로고    scopus 로고
    • Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy
    • Wang, Q., Zhuravleva, A., and Gierasch, L. M. (2011) Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy Biochemistry 50, 9225-9236
    • (2011) Biochemistry , vol.50 , pp. 9225-9236
    • Wang, Q.1    Zhuravleva, A.2    Gierasch, L.M.3
  • 48
    • 0035695918 scopus 로고    scopus 로고
    • Proteins in organic solvents
    • DOI 10.1016/S0959-440X(01)00278-0
    • Mattos, C. and Ringe, D. (2001) Proteins in organic solvents Curr. Opin. Struct. Biol. 11, 761-764 (Pubitemid 34076639)
    • (2001) Current Opinion in Structural Biology , vol.11 , Issue.6 , pp. 761-764
    • Mattos, C.1    Ringe, D.2
  • 49
    • 80055013471 scopus 로고    scopus 로고
    • Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy
    • Wang, Q., Zhuravleva, A., and Gierasch, L. M. (2011) Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell nuclear magnetic resonance spectroscopy Biochemistry 50, 9225-9236
    • (2011) Biochemistry , vol.50 , pp. 9225-9236
    • Wang, Q.1    Zhuravleva, A.2    Gierasch, L.M.3
  • 50
    • 79551523648 scopus 로고    scopus 로고
    • Macromolecule diffusion and confinement in prokaryotic cells
    • Mika, J. T. and Poolman, B. (2011) Macromolecule diffusion and confinement in prokaryotic cells Curr. Opin. Biotechnol. 22, 117-126
    • (2011) Curr. Opin. Biotechnol. , vol.22 , pp. 117-126
    • Mika, J.T.1    Poolman, B.2


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