메뉴 건너뛰기




Volumn 1840, Issue 9, 2014, Pages 2843-2850

Impact of protein and ligand impurities on ITC-derived protein-ligand thermodynamics

Author keywords

Dynamic light scattering; Enthalpy; Gibbs free energy; Impurities; Isothermal titration calorimetry

Indexed keywords

GLYCOSYLTRANSFERASE; QUEUINE TRANSFER RIBONUCLEIC ACID RIBOSYLTRANSFERASE; TRYPSIN; UNCLASSIFIED DRUG;

EID: 84903649557     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2014.04.018     Document Type: Article
Times cited : (18)

References (41)
  • 1
    • 35448962899 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: Experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions
    • M.W. Freyer, and E.A. Lewis Isothermal titration calorimetry: experimental design, data analysis, and probing macromolecule/ligand binding and kinetic interactions Methods Cell Biol. 84 2008 79 113
    • (2008) Methods Cell Biol. , vol.84 , pp. 79-113
    • Freyer, M.W.1    Lewis, E.A.2
  • 2
    • 48249102785 scopus 로고    scopus 로고
    • Calorimetry and thermodynamics in drug design
    • J.B. Chaires Calorimetry and thermodynamics in drug design Annu. Rev. Biophys. 37 2008 135 151
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 135-151
    • Chaires, J.B.1
  • 3
    • 0346022974 scopus 로고    scopus 로고
    • Understanding Protein-Ligand Interactions: The Price of Protein Flexibility
    • DOI 10.1016/j.jmb.2003.11.041
    • D. Rauh, G. Klebe, and M.T. Stubbs Understanding protein-ligand interactions: the price of protein flexibility J. Mol. Biol. 335 2004 1325 1341 (Pubitemid 38077249)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.5 , pp. 1325-1341
    • Rauh, D.1    Klebe, G.2    Stubbs, M.T.3
  • 4
    • 0041743079 scopus 로고    scopus 로고
    • ZZ made EZ: Influence of inhibitor configuration on enzyme selectivity
    • D. Rauh, G. Klebe, J. Stürzebecher, and M.T. Stubbs ZZ made EZ: influence of inhibitor configuration on enzyme selectivity J. Mol. Biol. 330 2003 761 770
    • (2003) J. Mol. Biol. , vol.330 , pp. 761-770
    • Rauh, D.1    Klebe, G.2    Stürzebecher, J.3    Stubbs, M.T.4
  • 5
    • 0036661079 scopus 로고    scopus 로고
    • Trypsin mutants for structure-based drug design: Expression, refolding and crystallisation
    • DOI 10.1515/BC.2002.148
    • D. Rauh, S. Reyda, G. Klebe, and M.T. Stubbs Trypsin mutants for structure-based drug design: expression, refolding and crystallisation Biol. Chem. 383 2002 1309 1314 (Pubitemid 35215083)
    • (2002) Biological Chemistry , vol.383 , Issue.7-8 , pp. 1309-1314
    • Rauh, D.1    Reyda, S.2    Klebe, G.3    Stubbs, M.T.4
  • 7
    • 0034255393 scopus 로고    scopus 로고
    • Lyophilization and development of solid protein pharmaceuticals
    • DOI 10.1016/S0378-5173(00)00423-3, PII S0378517300004233
    • W. Wang Lyophilization and development of solid protein pharmaceuticals Int. J. Pharm. 203 2000 1 60 (Pubitemid 30627625)
    • (2000) International Journal of Pharmaceutics , vol.203 , Issue.1-2 , pp. 1-60
    • Wang, W.1
  • 8
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • S.C. Gill, and P.H. von Hippel Calculation of protein extinction coefficients from amino acid sequence data Anal. Biochem. 182 1989 319 326 (Pubitemid 19277112)
    • (1989) Analytical Biochemistry , vol.182 , Issue.2 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 9
    • 0035172569 scopus 로고    scopus 로고
    • Rupture, invasion and inflammatory destruction of the intestinal barrier by Shigella, making sense of prokaryote-eukaryote cross-talks
    • DOI 10.1016/S0168-6445(00)00060-7, PII S0168644500000607
    • P.J. Sansonetti Rupture, invasion and inflammatory destruction of the intestinal barrier by Shigella, making sense of prokaryote-eukaryote cross-talks FEMS Microbiol. Rev. 25 2001 3 14 (Pubitemid 32057194)
    • (2001) FEMS Microbiology Reviews , vol.25 , Issue.1 , pp. 3-14
    • Sansonetti, P.J.1
  • 10
    • 0141596159 scopus 로고    scopus 로고
    • Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate
    • DOI 10.1038/nsb976
    • W. Xie, X. Liu, and R.H. Huang Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate Nat. Struct. Biol. 10 2003 781 788 (Pubitemid 37187647)
    • (2003) Nature Structural Biology , vol.10 , Issue.10 , pp. 781-788
    • Xie, W.1    Liu, X.2    Huang, R.H.3
  • 11
    • 0033965439 scopus 로고    scopus 로고
    • Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flexneri: The expression of the virF gene
    • DOI 10.1046/j.1365-2958.2000.01767.x
    • J.M.B. Durand, B. Dagberg, B.E. Uhlin, and G.R. Björk Transfer RNA modification, temperature and DNA superhelicity have a common target in the regulatory network of the virulence of Shigella flexneri: the expression of the virF gene Mol. Microbiol. 35 2000 924 935 (Pubitemid 30107542)
    • (2000) Molecular Microbiology , vol.35 , Issue.4 , pp. 924-935
    • Durand, J.M.B.1    Dagberg, B.2    Uhlin, B.E.3    Bjork, G.R.4
  • 12
    • 0029112199 scopus 로고
    • Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: Purification and biochemical characterization of the enzyme
    • K. Reuter, and R. Ficner Sequence analysis and overexpression of the Zymomonas mobilis tgt gene encoding tRNA-guanine transglycosylase: purification and biochemical characterization of the enzyme J. Bacteriol. 177 1995 5284 5288
    • (1995) J. Bacteriol. , vol.177 , pp. 5284-5288
    • Reuter, K.1    Ficner, R.2
  • 13
    • 0029897830 scopus 로고    scopus 로고
    • Purification, crystallization, and preliminary X-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilis
    • DOI 10.1002/(SICI)1097-0134(199604)24:4<516::AID-PROT11>3.0.CO;2-O
    • C. Romier, R. Ficner, K. Reuter, and D. Suck Purification, crystallization, and preliminary X-ray diffraction studies of tRNA-guanine transglycosylase from Zymomonas mobilis Proteins 24 1996 516 519 (Pubitemid 26122065)
    • (1996) Proteins: Structure, Function and Genetics , vol.24 , Issue.4 , pp. 516-519
    • Romier, C.1    Ficner, R.2    Reuter, K.3    Suck, D.4
  • 14
    • 36049041257 scopus 로고    scopus 로고
    • Potent inhibitors of tRNA-guanine transglycosylase, an enzyme linked to the pathogenicity of the Shigella bacterium: Charge-assisted hydrogen bonding
    • DOI 10.1002/anie.200702961
    • S.R. Hörtner, T. Ritschel, B. Stengl, C. Kramer, W.B. Schweizer, B. Wagner, M. Kansy, G. Klebe, and F. Diederich Potent inhibitors of tRNA-guanine transglycosylase, an enzyme linked to the pathogenicity of the Shigella bacterium: charge-assisted hydrogen bonding Angew. Chem. Int. Ed. 46 2007 8266 8269 (Angew. Chem., 119 (2007) 8414-8417) (Pubitemid 350096614)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.43 , pp. 8266-8269
    • Hortner, S.R.1    Ritschel, T.2    Stengl, B.3    Kramer, C.4    Schweizer, W.B.5    Wagner, B.6    Kansy, M.7    Klebe, G.8    Diederich, F.9
  • 15
    • 0017917984 scopus 로고
    • Protein concentration measurements: The dry weight
    • D.W. Kupke, and T.E. Dorrier Protein concentration measurements: the dry weight Methods Enzymol. 48 1978 155 162
    • (1978) Methods Enzymol. , vol.48 , pp. 155-162
    • Kupke, D.W.1    Dorrier, T.E.2
  • 16
    • 77049162117 scopus 로고
    • A micro biuret method for protein determination; Determination of total protein in cerebrospinal fluid
    • J. Goa A micro biuret method for protein determination; determination of total protein in cerebrospinal fluid Scand. J. Clin. Lab. Invest. 5 1953 218 222
    • (1953) Scand. J. Clin. Lab. Invest. , vol.5 , pp. 218-222
    • Goa, J.1
  • 17
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • A. Bensadoun, and D. Weinstein Assay of proteins in the presence of interfering materials Anal. Biochem. 70 1976 241 250
    • (1976) Anal. Biochem. , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 18
    • 0017179210 scopus 로고
    • a's of aspartyl-102 and aspartyl-194 in bovine trypsin using difference infrared spectroscopy
    • a's of aspartyl-102 and aspartyl-194 in bovine trypsin using difference infrared spectroscopy Biochemistry 15 1976 3450 3458
    • (1976) Biochemistry , vol.15 , pp. 3450-3458
    • Koeppe, R.E.1    Stroud, R.M.2
  • 21
    • 0017184389 scopus 로고
    • Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding
    • M.M. Bradford Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0842303040 scopus 로고    scopus 로고
    • The role of backlash in the "first injection anomaly" in isothermal titration calorimetry
    • DOI 10.1016/j.ab.2003.10.048
    • L.S. Mizoue, and J. Tellinghuisen The role of backlash in the "first injection anomaly" in isothermal titration calorimetry Anal. Biochem. 326 2004 125 127 (Pubitemid 38177493)
    • (2004) Analytical Biochemistry , vol.326 , Issue.1 , pp. 125-127
    • Mizoue, L.S.1    Tellinghuisen, J.2
  • 23
    • 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
    • T. Wiseman, S. Williston, J.F. Brandts, and L.N. Lin Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179 1989 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
  • 24
    • 0034953839 scopus 로고    scopus 로고
    • Making cool drugs hot: Isothermal titration calorimetry as a tool to study binding energetics
    • G.A. Holdgate Making cool drugs hot: isothermal titration calorimetry as a tool to study binding energetics Biotechniques 31 2001 164 184 (Pubitemid 32645923)
    • (2001) BioTechniques , vol.31 , Issue.1 , pp. 164-184
    • Holdgate, G.A.1
  • 25
    • 4444275437 scopus 로고    scopus 로고
    • Zur Lehre von der Wirkung der Salze (about the science of the effect of salts): Franz Hofmeister's historical papers
    • DOI 10.1016/j.cocis.2004.05.005, PII S1359029404000317
    • W. Kunz, J. Henle, and B.W. Ninham 'Zur Lehre von der Wirkung der Salze' (about the science of the effect of salts): Franz Hofmeister's historical papers Curr. Opin. Colloid Interf. Sci. 9 2004 19 37 (Pubitemid 39194131)
    • (2004) Current Opinion in Colloid and Interface Science , vol.9 , Issue.1-2 , pp. 19-37
    • Kunz, W.1    Henle, J.2    Ninham, B.W.3
  • 26
    • 0037061628 scopus 로고    scopus 로고
    • A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening
    • DOI 10.1021/jm010533y
    • S.L. McGovern, E. Caselli, N. Grigorieff, and B.K. Shoichet A common mechanism underlying promiscuous inhibitors from virtual and high-throughput screening J. Med. Chem. 45 2002 1712 1722 (Pubitemid 34293537)
    • (2002) Journal of Medicinal Chemistry , vol.45 , Issue.8 , pp. 1712-1722
    • McGovern, S.L.1    Caselli, E.2    Grigorieff, N.3    Shoichet, B.K.4
  • 27
    • 84925559007 scopus 로고    scopus 로고
    • Protein sample characterization
    • T. Daviter, and R. Fronzes Protein sample characterization Methods Mol. Biol. 1008 2013 35 62
    • (2013) Methods Mol. Biol. , vol.1008 , pp. 35-62
    • Daviter, T.1    Fronzes, R.2
  • 28
    • 0002604494 scopus 로고    scopus 로고
    • Needs for standards in isothermal microcalorimetry
    • I. Wadsö Needs for standards in isothermal microcalorimetry Thermochim. Acta 347 2000 73 77
    • (2000) Thermochim. Acta , vol.347 , pp. 73-77
    • Wadsö, I.1
  • 29
    • 33845437051 scopus 로고    scopus 로고
    • Calibration in isothermal titration calorimetry: Heat and cell volume from heat of dilution of NaCl(aq)
    • DOI 10.1016/j.ab.2006.10.015, PII S0003269706007597
    • J. Tellinghuisen Calibration in isothermal titration calorimetry: heat and cell volume from heat of dilution of NaCl(aq) Anal. Biochem. 360 2007 47 55 (Pubitemid 44894350)
    • (2007) Analytical Biochemistry , vol.360 , Issue.1 , pp. 47-55
    • Tellinghuisen, J.1
  • 30
    • 67649649592 scopus 로고    scopus 로고
    • Titration calorimetry standards and the precision of isothermal titration calorimetry data
    • L. Baranauskiene, V. Petrikaite, J. Matuliene, and D. Matulis Titration calorimetry standards and the precision of isothermal titration calorimetry data Int. J. Mol. Sci. 10 2009 2752 2762
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 2752-2762
    • Baranauskiene, L.1    Petrikaite, V.2    Matuliene, J.3    Matulis, D.4
  • 31
    • 0345293146 scopus 로고    scopus 로고
    • On the Value of c: Can Low Affinity Systems Be Studied by Isothermal Titration Calorimetry?
    • DOI 10.1021/ja036166s
    • W.B. Turnbull, and A.H. Daranas On the value of c: can low affinity systems be studied by isothermal titration calorimetry? J. Am. Chem. Soc. 125 2003 14859 14866 (Pubitemid 37475576)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.48 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 32
    • 79956145674 scopus 로고    scopus 로고
    • Systematic errors in isothermal titration calorimetry: Concentrations and baselines
    • J. Tellinghuisen, and J.D. Chodera Systematic errors in isothermal titration calorimetry: concentrations and baselines Anal. Biochem. 414 2011 297 299
    • (2011) Anal. Biochem. , vol.414 , pp. 297-299
    • Tellinghuisen, J.1    Chodera, J.D.2
  • 33
    • 27744569982 scopus 로고    scopus 로고
    • Optimizing experimental parameters in isothermal titration calorimetry
    • DOI 10.1021/jp053550y
    • J. Tellinghuisen Optimizing experimental parameters in isothermal titration calorimetry J. Phys. Chem. B 109 2005 20027 20035 (Pubitemid 41598517)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.42 , pp. 20027-20035
    • Tellinghuisen, J.1
  • 35
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • A. Velazquez-Campoy, and E. Freire Isothermal titration calorimetry to determine association constants for high-affinity ligands Nat. Protoc. 1 2006 186 191
    • (2006) Nat. Protoc. , vol.1 , pp. 186-191
    • Velazquez-Campoy, A.1    Freire, E.2
  • 36
    • 69549137853 scopus 로고    scopus 로고
    • Analysis of cooperativity by isothermal titration calorimetry
    • A. Brown Analysis of cooperativity by isothermal titration calorimetry Int. J. Mol. Sci. 10 2009 3457 3477
    • (2009) Int. J. Mol. Sci. , vol.10 , pp. 3457-3477
    • Brown, A.1
  • 37
    • 47549106882 scopus 로고    scopus 로고
    • Applications of isothermal titration calorimetry in protein science
    • DOI 10.1111/j.1745-7270.2008.00437.x
    • Y. Liang Applications of isothermal titration calorimetry in protein science Acta Biochim. Biophys. Sin. 40 2008 565 576 (Pubitemid 352009079)
    • (2008) Acta Biochimica et Biophysica Sinica , vol.40 , Issue.7 , pp. 565-576
    • Liang, Y.1
  • 38
    • 0042831474 scopus 로고    scopus 로고
    • A study of statistical error in isothermal titration calorimetry
    • DOI 10.1016/S0003-2697(03)00406-8
    • J. Tellinghuisen A study of statistical error in isothermal titration calorimetry Anal. Biochem. 321 2003 79 88 (Pubitemid 37083269)
    • (2003) Analytical Biochemistry , vol.321 , Issue.1 , pp. 79-88
    • Tellinghuisen, J.1
  • 39
    • 1642546385 scopus 로고    scopus 로고
    • Statistical Error in Isothermal Titration Calorimetry
    • DOI 10.1016/S0076-6879(04)83011-8
    • J. Tellinghuisen Statistical error in isothermal titration calorimetry Methods Enzymol. 383 2004 245 282 (Pubitemid 38401794)
    • (2004) Methods in Enzymology , vol.383 , pp. 245-282
    • Tellinghuisen, J.1
  • 41
    • 84873351927 scopus 로고    scopus 로고
    • Dissecting the hydrophobic effect on the molecular level: The role of water, enthalpy, and entropy in ligand binding to thermolysin
    • A. Biela, N.N. Nasief, M. Betz, A. Heine, D. Hangauer, and G. Klebe Dissecting the hydrophobic effect on the molecular level: the role of water, enthalpy, and entropy in ligand binding to thermolysin Angew. Chem. Int. Ed. 52 2013 1822 1828
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 1822-1828
    • Biela, A.1    Nasief, N.N.2    Betz, M.3    Heine, A.4    Hangauer, D.5    Klebe, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.