메뉴 건너뛰기




Volumn 11, Issue 5, 2016, Pages 882-894

Integration and global analysis of isothermal titration calorimetry data for studying macromolecular interactions

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BINDING COMPETITION; CHEMICAL BINDING; CHEMICAL INTERACTION; DATA ANALYSIS; DATA ANALYSIS SOFTWARE; FLUORESCENCE POLARIZATION; ISOTHERM; ISOTHERMAL TITRATION CALORIMETRY; LIMIT OF QUANTITATION; MACROMOLECULE; NOISE; PRIORITY JOURNAL; SEDIMENTATION RATE; STATISTICAL ANALYSIS; SURFACE PLASMON RESONANCE; THERMOGRAPHY; CALORIMETRY; CHEMISTRY; COMPUTER PROGRAM; MARKOV CHAIN; PROCEDURES; SIGNAL PROCESSING; STATISTICS AND NUMERICAL DATA;

EID: 84983542776     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2016.044     Document Type: Article
Times cited : (207)

References (60)
  • 1
    • 37249065351 scopus 로고    scopus 로고
    • The molecular sociology of the cell
    • Robinson, C.V., Sali, A. & Baumeister, W. The molecular sociology of the cell. Nature 450, 973-982 (2007).
    • (2007) Nature , vol.450 , pp. 973-982
    • Robinson, C.V.1    Sali, A.2    Baumeister, W.3
  • 2
    • 76649135799 scopus 로고    scopus 로고
    • Signalling complexes and clusters: Functional advantages and methodological hurdles
    • Cebecauer, M., Spitaler, M., Sergé, A. & Magee, A.I. Signalling complexes and clusters: functional advantages and methodological hurdles. J. Cell Sci. 123, 309-320 (2010).
    • (2010) J. Cell Sci , vol.123 , pp. 309-320
    • Cebecauer, M.1    Spitaler, M.2    Sergé, A.3    Magee, A.I.4
  • 3
    • 84860527594 scopus 로고    scopus 로고
    • Noise in cellular signaling pathways: Causes and effects
    • Ladbury, J.E. & Arold, S.T. Noise in cellular signaling pathways: causes and effects. Trends Biochem. Sci. 37, 173-178 (2012).
    • (2012) Trends Biochem. Sci , vol.37 , pp. 173-178
    • Ladbury, J.E.1    Arold, S.T.2
  • 4
    • 74149083849 scopus 로고    scopus 로고
    • Adding calorimetric data to decision making in lead discovery: A hot tip
    • Ladbury, J.E., Klebe, G. & Freire, E. Adding calorimetric data to decision making in lead discovery: a hot tip. Nat. Rev. Drug Discov. 9, 23-27 (2010).
    • (2010) Nat. Rev. Drug Discov , vol.9 , pp. 23-27
    • Ladbury, J.E.1    Klebe, G.2    Freire, E.3
  • 5
    • 48249102785 scopus 로고    scopus 로고
    • Calorimetry and thermodynamics in drug design
    • Chaires, J.B. Calorimetry and thermodynamics in drug design. Annu. Rev. Biophys. 37, 135-151 (2008).
    • (2008) Annu. Rev. Biophys , vol.37 , pp. 135-151
    • Chaires, J.B.1
  • 6
    • 27244462844 scopus 로고
    • Isothermal titration calorimetry
    • Freire, E., Mayorga, O.L. & Straume, M. Isothermal titration calorimetry. Anal. Chem. 62, 950A-959A (1990).
    • (1990) Anal. Chem , vol.62 , pp. 950A-959A
    • Freire, E.1    Mayorga, O.L.2    Straume, M.3
  • 7
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., Williston, S., Brandts, J.F. & Lin, L.N. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 179, 131-137 (1989).
    • (1989) Anal. Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 8
    • 0031627006 scopus 로고    scopus 로고
    • Microcalorimetry of protein-protein interactions
    • Cooper, A. Microcalorimetry of protein-protein interactions. Methods Mol. Biol. 88, 11-22 (1998).
    • (1998) Methods Mol. Biol , vol.88 , pp. 11-22
    • Cooper, A.1
  • 9
    • 83755168898 scopus 로고    scopus 로고
    • Molecular structure encodes nanoscale assemblies: Understanding driving forces in electrostatic self-assembly
    • Willerich, I. & Gröhn, F. Molecular structure encodes nanoscale assemblies: understanding driving forces in electrostatic self-assembly. J. Am. Chem. Soc. 133, 20341-20356 (2011).
    • (2011) J. Am. Chem. Soc , vol.133 , pp. 20341-20356
    • Willerich, I.1    Gröhn, F.2
  • 10
    • 67649412187 scopus 로고    scopus 로고
    • Monitoring detergent-mediated solubilization and reconstitution of lipid membranes by isothermal titration calorimetry
    • Heerklotz, H., Tsamaloukas, A.D. & Keller, S. Monitoring detergent-mediated solubilization and reconstitution of lipid membranes by isothermal titration calorimetry. Nat. Protoc. 4, 686-697 (2009).
    • (2009) Nat. Protoc , vol.4 , pp. 686-697
    • Heerklotz, H.1    Tsamaloukas, A.D.2    Keller, S.3
  • 11
    • 34347238617 scopus 로고    scopus 로고
    • And release protocol for assessing membrane binding and permeation by way of isothermal titration calorimetry
    • Tsamaloukas, A.D., Keller, S. & Heerklotz, H. Uptake and release protocol for assessing membrane binding and permeation by way of isothermal titration calorimetry. Nat. Protoc. 2, 695-704 (2007).
    • (2007) Nat. Protoc , vol.2 , pp. 695-704
    • Tsamaloukas, A.D.1    Keller, S.2    Uptake, H.H.3
  • 12
    • 0026059557 scopus 로고
    • Calorimetric determination of cooperative interactions in high affinity binding processes
    • Bains, G. & Freire, E. Calorimetric determination of cooperative interactions in high affinity binding processes. Anal. Biochem. 192, 203-206 (1991).
    • (1991) Anal. Biochem , vol.192 , pp. 203-206
    • Bains, G.1    Freire, E.2
  • 13
    • 69549137853 scopus 로고    scopus 로고
    • Analysis of cooperativity by isothermal titration calorimetry
    • Brown, A. Analysis of cooperativity by isothermal titration calorimetry. Int. J. Mol. Sci. 10, 3457-3477 (2009).
    • (2009) Int. J. Mol. Sci , vol.10 , pp. 3457-3477
    • Brown, A.1
  • 14
    • 61849095281 scopus 로고    scopus 로고
    • Isothermal titration calorimetry: General formalism using binding polynomials
    • Freire, E., Schön, A. & Velázquez-Campoy, A. Isothermal titration calorimetry: general formalism using binding polynomials. Methods Enzymol. 455, 127-155 (2009).
    • (2009) Methods Enzymol , vol.455 , pp. 127-155
    • Freire, E.1    Schön, A.2    Velázquez-Campoy, A.3
  • 15
    • 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
    • Houtman, J.C.D. et al. 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 (2007).
    • (2007) Protein Sci , vol.16 , pp. 30-42
    • Houtman, J.C.D.1
  • 16
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
    • Baker, B.M. & Murphy, K.P. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys. J. 71, 2049-2055 (1996).
    • (1996) Biophys. J , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 17
    • 84862799382 scopus 로고    scopus 로고
    • Strategies for assessing proton linkage to bimolecular interactions by global analysis of isothermal titration calorimetry data
    • Coussens, N.P., Schuck, P. & Zhao, H. Strategies for assessing proton linkage to bimolecular interactions by global analysis of isothermal titration calorimetry data. J. Chem. Thermodyn. 52, 95-107 (2012).
    • (2012) J. Chem. Thermodyn , vol.52 , pp. 95-107
    • Coussens, N.P.1    Schuck, P.2    Zhao, H.3
  • 18
    • 84861840835 scopus 로고    scopus 로고
    • High-precision isothermal titration calorimetry with automated peak shape analysis
    • Keller, S. et al. High-precision isothermal titration calorimetry with automated peak shape analysis. Anal. Chem. 84, 5066-5073 (2012).
    • (2012) Anal. Chem , vol.84 , pp. 5066-5073
    • Keller, S.1
  • 19
    • 0032720338 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of protein-protein interactions
    • Pierce, M.M., Raman, C.S. & Nall, B.T. Isothermal titration calorimetry of protein-protein interactions. Methods 19, 213-221 (1999).
    • (1999) Methods , vol.19 , pp. 213-221
    • Pierce, M.M.1    Raman, C.S.2    Nall, B.T.3
  • 20
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • Velázquez-Campoy, A. & Freire, E. Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nat. Protoc. 1, 186-191 (2006).
    • (2006) Nat. Protoc , vol.1 , pp. 186-191
    • Velázquez-Campoy, A.1    Freire, E.2
  • 21
    • 75649115763 scopus 로고    scopus 로고
    • Recent trends and some applications of isothermal titration calorimetry in biotechnology
    • Roselin, L.S., Lin, M.-S., Lin, P.-H., Chang, Y. & Chen, W.-Y. Recent trends and some applications of isothermal titration calorimetry in biotechnology. Biotechnol. J. 5, 85-98 (2010).
    • (2010) Biotechnol. J , vol.5 , pp. 85-98
    • Roselin, L.S.1    Lin, M.-S.2    Lin, P.-H.3    Chang, Y.4    Chen, W.-Y.5
  • 24
    • 84925445801 scopus 로고    scopus 로고
    • High-precision automated integration of multiple isothermal titration calorimetric thermograms: New features of NITPIC
    • Scheuermann, T.H. & Brautigam, C.A. High-precision, automated integration of multiple isothermal titration calorimetric thermograms: new features of NITPIC. Methods 76, 87-98 (2015).
    • (2015) Methods , vol.76 , pp. 87-98
    • Scheuermann, T.H.1    Brautigam, C.A.2
  • 25
    • 70350050570 scopus 로고    scopus 로고
    • Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 1. Calorimetric study
    • Herman, P. & Lee, J.C. Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 1. Calorimetric study. Biochemistry 48, 9448-9455 (2009).
    • (2009) Biochemistry , vol.48 , pp. 9448-9455
    • Herman, P.1    Lee, J.C.2
  • 26
    • 80155128011 scopus 로고    scopus 로고
    • Open-ITC: An alternate computational approach to analyze the isothermal titration calorimetry data of complex binding mechanisms
    • Krishnamoorthy, J. & Mohanty, S. Open-ITC: an alternate computational approach to analyze the isothermal titration calorimetry data of complex binding mechanisms. J. Mol. Recognit. 24, 1056-1066 (2011).
    • (2011) J. Mol. Recognit , vol.24 , pp. 1056-1066
    • Krishnamoorthy, J.1    Mohanty, S.2
  • 27
    • 61849154739 scopus 로고    scopus 로고
    • Characterization of parvalbumin and polcalcin divalent ion binding by isothermal titration calorimetry
    • Henzl, M.T. Characterization of parvalbumin and polcalcin divalent ion binding by isothermal titration calorimetry. Methods Enzymol. 455, 259-297 (2009).
    • (2009) Methods Enzymol , vol.455 , pp. 259-297
    • Henzl, M.T.1
  • 28
    • 72949117250 scopus 로고    scopus 로고
    • Elucidating protein binding mechanisms by variable-c ITC
    • Freiburger, L.A., Auclair, K. & Mittermaier, A.K. Elucidating protein binding mechanisms by variable-c ITC. Chembiochem 10, 2871-2873 (2009).
    • (2009) Chembiochem , vol.10 , pp. 2871-2873
    • Freiburger, L.A.1    Auclair, K.2    Mittermaier, A.K.3
  • 29
    • 84857837683 scopus 로고    scopus 로고
    • Higher order inclusion complexes and secondary interactions studied by global analysis of calorimetric titrations
    • Schönbeck, C., Holm, R. & Westh, P. Higher order inclusion complexes and secondary interactions studied by global analysis of calorimetric titrations. Anal. Chem. 84, 2305-2312 (2012).
    • (2012) Anal. Chem , vol.84 , pp. 2305-2312
    • Schönbeck, C.1    Holm, R.2    Westh, P.3
  • 30
    • 84925455000 scopus 로고    scopus 로고
    • SEDPHAT-A platform for global ITC analysis and global multi-method analysis of molecular interactions
    • Zhao, H., Piszczek, G. & Schuck, P. SEDPHAT-A platform for global ITC analysis and global multi-method analysis of molecular interactions. Methods 76, 137-148 (2015).
    • (2015) Methods , vol.76 , pp. 137-148
    • Zhao, H.1    Piszczek, G.2    Schuck, P.3
  • 31
    • 34447299949 scopus 로고    scopus 로고
    • A comprehensive calorimetric investigation of an entropically driven T cell receptor-peptide/major histocompatibility complex interaction
    • Armstrong, K.M. & Baker, B.M. A comprehensive calorimetric investigation of an entropically driven T cell receptor-peptide/major histocompatibility complex interaction. Biophys. J. 93, 597-609 (2007).
    • (2007) Biophys. J , vol.93 , pp. 597-609
    • Armstrong, K.M.1    Baker, B.M.2
  • 32
    • 79952361572 scopus 로고    scopus 로고
    • Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme
    • Freiburger, L.A. et al. Competing allosteric mechanisms modulate substrate binding in a dimeric enzyme. Nat. Struct. Mol. Biol. 18, 288-294 (2011).
    • (2011) Nat. Struct. Mol. Biol , vol.18 , pp. 288-294
    • Freiburger, L.A.1
  • 33
    • 70350074063 scopus 로고    scopus 로고
    • Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 2. Fluorescence study
    • Herman, P. & Lee, J.C. Functional energetic landscape in the allosteric regulation of muscle pyruvate kinase. 2. Fluorescence study. Biochemistry 48, 9456-9465 (2009).
    • (2009) Biochemistry , vol.48 , pp. 9456-9465
    • Herman, P.1    Lee, J.C.2
  • 34
    • 84868532699 scopus 로고    scopus 로고
    • Global multi-method analysis of affinities and cooperativity in complex systems of macromolecular interactions
    • Zhao, H. & Schuck, P. Global multi-method analysis of affinities and cooperativity in complex systems of macromolecular interactions. Anal. Chem. 84, 9513-9519 (2012).
    • (2012) Anal. Chem , vol.84 , pp. 9513-9519
    • Zhao, H.1    Schuck, P.2
  • 35
    • 84921810067 scopus 로고    scopus 로고
    • Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT
    • Zhao, H. & Schuck, P. Combining biophysical methods for the analysis of protein complex stoichiometry and affinity in SEDPHAT. Acta Crystallogr. D Biol. Crystallogr. 71, 3-14 (2015).
    • (2015) Acta Crystallogr. D Biol. Crystallogr , vol.71 , pp. 3-14
    • Zhao, H.1    Schuck, P.2
  • 36
    • 84925440551 scopus 로고    scopus 로고
    • Global ITC fitting methods in studies of protein allostery
    • Freiburger, L., Auclair, K. & Mittermaier, A. Global ITC fitting methods in studies of protein allostery. Methods 76, 149-161 (2015).
    • (2015) Methods , vol.76 , pp. 149-161
    • Freiburger, L.1    Auclair, K.2    Mittermaier, A.3
  • 37
    • 33748366578 scopus 로고    scopus 로고
    • Oligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1
    • Houtman, J.C.D. et al. Oligomerization of signaling complexes by the multipoint binding of GRB2 to both LAT and SOS1. Nat. Struct. Mol. Biol. 13, 798-805 (2006).
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 798-805
    • Houtman, J.C.D.1
  • 38
    • 84863386821 scopus 로고    scopus 로고
    • And biochemical characterization of human mitochondrial branched-chain α-ketoacid dehydrogenase phosphatase
    • Wynn, R.M., Li, J., Brautigam, C.A., Chuang, J.L. & Chuang, D.T. Structural and biochemical characterization of human mitochondrial branched-chain α-ketoacid dehydrogenase phosphatase. J. Biol. Chem. 287, 9178-9192 (2012).
    • (2012) J. Biol. Chem , vol.287 , pp. 9178-9192
    • Wynn, R.M.1    Li, J.2    Brautigam, C.A.3    Chuang, J.L.4    Structural, T.C.D.5
  • 39
    • 84858626900 scopus 로고    scopus 로고
    • Weak interactions between folate and osmolytes in solution
    • Duff, M.R., Grubbs, J., Serpersu, E. & Howell, E.E. Weak interactions between folate and osmolytes in solution. Biochemistry 51, 2309-2318 (2012).
    • (2012) Biochemistry , vol.51 , pp. 2309-2318
    • Duff, M.R.1    Grubbs, J.2    Serpersu, E.3    Howell, E.E.4
  • 40
    • 78649970557 scopus 로고    scopus 로고
    • Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch
    • Huang, L., Serganov, A. & Patel, D.J. Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch. Mol. Cell 40, 774-786 (2010).
    • (2010) Mol. Cell , vol.40 , pp. 774-786
    • Huang, L.1    Serganov, A.2    Patel, D.J.3
  • 41
    • 84892379392 scopus 로고    scopus 로고
    • Complexes of neutralizing and non-neutralizing affinity matured Fabs with a mimetic of the internal trimeric coiled-coil of HIV-1 gp41
    • Gustchina, E. et al. Complexes of neutralizing and non-neutralizing affinity matured Fabs with a mimetic of the internal trimeric coiled-coil of HIV-1 gp41. PLoS One 8, e78187 (2013).
    • (2013) PLoS One , vol.8 , pp. e78187
    • Gustchina, E.1
  • 42
    • 78650902377 scopus 로고    scopus 로고
    • Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site
    • Dellarole, M., Sánchez, I.E. & de Prat Gay, G. Thermodynamics of cooperative DNA recognition at a replication origin and transcription regulatory site. Biochemistry 49, 10277-10286 (2010).
    • (2010) Biochemistry , vol.49 , pp. 10277-10286
    • Dellarole, M.1    Sánchez, I.E.2    De Prat Gay, G.3
  • 43
    • 84871265987 scopus 로고    scopus 로고
    • Quantifying high-affinity binding of hydrophobic ligands by isothermal titration calorimetry
    • Krainer, G., Broecker, J., Vargas, C., Fanghänel, J. & Keller, S. Quantifying high-affinity binding of hydrophobic ligands by isothermal titration calorimetry. Anal. Chem. 84, 10715-10722 (2012).
    • (2012) Anal. Chem , vol.84 , pp. 10715-10722
    • Krainer, G.1    Broecker, J.2    Vargas, C.3    Fanghänel, J.4    Keller, S.5
  • 44
    • 57749089751 scopus 로고    scopus 로고
    • Assembly of oligomeric death domain complexes during Toll receptor signaling
    • Moncrieffe, M.C., Grossmann, J.G. & Gay, N.J. Assembly of oligomeric death domain complexes during Toll receptor signaling. J. Biol. Chem. 283, 33447-33454 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 33447-33454
    • Moncrieffe, M.C.1    Grossmann, J.G.2    Gay, N.J.3
  • 45
    • 77649274109 scopus 로고    scopus 로고
    • New insights into the mechanism of dihydrodipicolinate synthase using isothermal titration calorimetry
    • Muscroft-Taylor, A.C., Soares da Costa, T.P. & Gerrard, J.A. New insights into the mechanism of dihydrodipicolinate synthase using isothermal titration calorimetry. Biochimie 92, 254-262 (2010).
    • (2010) Biochimie , vol.92 , pp. 254-262
    • Muscroft-Taylor, A.C.1    Soares da Costa, T.P.2    Gerrard, J.A.3
  • 46
    • 83755173208 scopus 로고    scopus 로고
    • Conformer-independent ureidoimidazole motifs-tools to probe conformational and tautomeric effects on the molecular recognition of triply hydrogen-bonded heterodimers
    • Pellizzaro, M.L. et al. Conformer-independent ureidoimidazole motifs-tools to probe conformational and tautomeric effects on the molecular recognition of triply hydrogen-bonded heterodimers. Chem. Eur. J. 17, 14508-14517 (2011).
    • (2011) Chem. Eur. J , vol.17 , pp. 14508-14517
    • Pellizzaro, M.L.1
  • 47
    • 84925449320 scopus 로고    scopus 로고
    • Single-experiment displacement assay for quantifying high-affinity binding by isothermal titration calorimetry
    • Krainer, G. & Keller, S. Single-experiment displacement assay for quantifying high-affinity binding by isothermal titration calorimetry. Methods 76, 116-123 (2015).
    • (2015) Methods , vol.76 , pp. 116-123
    • Krainer, G.1    Keller, S.2
  • 48
    • 84948575628 scopus 로고    scopus 로고
    • Calculations and publication-quality illustrations for analytical ultracentrifugation data
    • Brautigam, C.A. Calculations and publication-quality illustrations for analytical ultracentrifugation data. Methods Enzymol. 562, 109-133 (2015).
    • (2015) Methods Enzymol , vol.562 , pp. 109-133
    • Brautigam, C.A.1
  • 49
    • 84874533137 scopus 로고    scopus 로고
    • Intrinsic thermodynamics of ethoxzolamide inhibitor binding to human carbonic anhydrase XIII
    • Baranauskiene, L. & Matulis, D. Intrinsic thermodynamics of ethoxzolamide inhibitor binding to human carbonic anhydrase XIII. BMC Biophys. 5, 12 (2012).
    • (2012) BMC Biophys , vol.5 , pp. 12
    • Baranauskiene, L.1    Matulis, D.2
  • 51
    • 80052769856 scopus 로고    scopus 로고
    • Revisiting the optimal c value for isothermal titration calorimetry
    • Broecker, J., Vargas, C. & Keller, S. Revisiting the optimal c value for isothermal titration calorimetry. Anal. Biochem. 418, 307-309 (2011).
    • (2011) Anal. Biochem , vol.418 , pp. 307-309
    • Broecker, J.1    Vargas, C.2    Keller, S.3
  • 52
    • 43349088689 scopus 로고    scopus 로고
    • Simultaneous calculation of equilibrium constants and standard formation enthalpies from calorimetric data for systems with multiple equilibria in solution
    • Gans, P., Sabatini, A. & Vacca, A. Simultaneous calculation of equilibrium constants and standard formation enthalpies from calorimetric data for systems with multiple equilibria in solution. J. Solution Chem. 37, 467-476 (2008).
    • (2008) J. Solution Chem , vol.37 , pp. 467-476
    • Gans, P.1    Sabatini, A.2    Vacca, A.3
  • 53
    • 84925405686 scopus 로고    scopus 로고
    • Fitting two- and three-site binding models to isothermal titration calorimetric data
    • Brautigam, C.A. Fitting two- and three-site binding models to isothermal titration calorimetric data. Methods 76, 124-136 (2015).
    • (2015) Methods , vol.76 , pp. 124-136
    • Brautigam, C.A.1
  • 54
    • 84925436890 scopus 로고    scopus 로고
    • A unified framework based on the binding polynomial for characterizing biological systems by isothermal titration calorimetry
    • Vega, S., Abian, O. & Velázquez-Campoy, A. A unified framework based on the binding polynomial for characterizing biological systems by isothermal titration calorimetry. Methods 76, 99-115 (2015).
    • (2015) Methods , vol.76 , pp. 99-115
    • Vega, S.1    Abian, O.2    Velázquez-Campoy, A.3
  • 55
    • 84880848925 scopus 로고    scopus 로고
    • Differential binding models for isothermal titration calorimetry: Moving beyond the Wiseman isotherm
    • Herrera, I. & Winnik, M. Differential binding models for isothermal titration calorimetry: moving beyond the Wiseman isotherm. J. Phys. Chem. B 117, 8659-8672 (2013).
    • (2013) J. Phys. Chem. B , vol.117 , pp. 8659-8672
    • Herrera, I.1    Winnik, M.2
  • 57
    • 0035981605 scopus 로고    scopus 로고
    • Thermodynamic quantities for the ionization reactions of buffers
    • Goldberg, R., Kishore, N. & Lennen, R.M. Thermodynamic quantities for the ionization reactions of buffers. J. Phys. Chem. Ref. Data 31, 231-370 (1999).
    • (1999) J. Phys. Chem. Ref. Data , vol.31 , pp. 231-370
    • Goldberg, R.1    Kishore, N.2    Lennen, R.M.3
  • 59
    • 84925457850 scopus 로고    scopus 로고
    • Calorimetric quantification of linked equilibria in cyclodextrin/lipid/detergent mixtures for membrane-protein reconstitution
    • Textor, M., Vargas, C. & Keller, S. Calorimetric quantification of linked equilibria in cyclodextrin/lipid/detergent mixtures for membrane-protein reconstitution. Methods 76, 183-193 (2015).
    • (2015) Methods , vol.76 , pp. 183-193
    • Textor, M.1    Vargas, C.2    Keller, S.3
  • 60
    • 84954362738 scopus 로고    scopus 로고
    • Calorimetric quantification of cyclodextrin-mediated detergent extraction for membrane-protein reconstitution
    • Textor, M. & Keller, S. Calorimetric quantification of cyclodextrin-mediated detergent extraction for membrane-protein reconstitution. Methods Enzymol. 567, 129-156 (2016).
    • (2016) Methods Enzymol , vol.567 , pp. 129-156
    • Textor, M.1    Keller, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.