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Volumn 40, Issue 7, 2008, Pages 565-576

Applications of isothermal titration calorimetry in protein science

Author keywords

Isothermal titration calorimetry; Protein folding; Protein interaction; Protein misfolding; Thermodynamics

Indexed keywords

PROTEIN;

EID: 47549106882     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1111/j.1745-7270.2008.00437.x     Document Type: Review
Times cited : (69)

References (46)
  • 1
    • 8444250720 scopus 로고    scopus 로고
    • A survey of the year 2003 literature on applications of isothermal titration calorimetry
    • Cliff MJ, Gutierrez A, Ladbury JE. A survey of the year 2003 literature on applications of isothermal titration calorimetry. J Mol Recognit 2004, 17 : 513 523
    • (2004) J Mol Recognit , vol.17 , pp. 513-523
    • Cliff, M.J.1    Gutierrez, A.2    Ladbury, J.E.3
  • 2
    • 31144454672 scopus 로고    scopus 로고
    • Survey of the year 2004: Literature on applications of isothermal titration calorimetry
    • Ababou A, Ladbury JE. Survey of the year 2004: literature on applications of isothermal titration calorimetry. J Mol Recognit 2006, 19 : 79 89
    • (2006) J Mol Recognit , vol.19 , pp. 79-89
    • Ababou, A.1    Ladbury, J.E.2
  • 3
    • 33846527387 scopus 로고    scopus 로고
    • A survey of the year 2005 literature on applications of isothermal titration calorimetry
    • Ababou A, Ladbury JE. A survey of the year 2005 literature on applications of isothermal titration calorimetry. J Mol Recognit 2007, 20 : 4 14
    • (2007) J Mol Recognit , vol.20 , pp. 4-14
    • Ababou, A.1    Ladbury, J.E.2
  • 4
    • 39749105201 scopus 로고    scopus 로고
    • A survey of the year 2006 literature on applications of isothermal titration calorimetry
    • Okhrimenkoa O, Jelesarov I. A survey of the year 2006 literature on applications of isothermal titration calorimetry. J Mol Recognit 2008, 21 : 1 19
    • (2008) J Mol Recognit , vol.21 , pp. 1-19
    • Okhrimenkoa, O.1    Jelesarov, I.2
  • 5
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
    • Baker BM, Murphy KP. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys J 1996, 71 : 2049 2055
    • (1996) Biophys J , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 6
    • 0025293251 scopus 로고
    • Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry
    • Connelly PR, Varadarajan R, Sturtevant JM, Richards FM. Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry. Biochemistry 1990, 29 : 6108 6114
    • (1990) Biochemistry , vol.29 , pp. 6108-6114
    • Connelly, P.R.1    Varadarajan, R.2    Sturtevant, J.M.3    Richards, F.M.4
  • 7
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar RS, Record MT Jr. Coupling of local folding to site-specific binding of proteins to DNA. Science 1994, 263 : 777 784
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record Jr., M.T.2
  • 8
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen CB. Principles that govern the folding of protein chains. Science 1973, 181 : 223 230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 9
    • 0043032426 scopus 로고    scopus 로고
    • Unfolding of rabbit muscle creatine kinase induced by acid. a study using electrospray ionization mass spectrometry, isothermal titration calorimetry, and fluorescence spectroscopy
    • Liang Y, Du F, Sanglier S, Zhou BR, Xia Y, Va n Dorsselaer A, Maechling C et al. Unfolding of rabbit muscle creatine kinase induced by acid. A study using electrospray ionization mass spectrometry, isothermal titration calorimetry, and fluorescence spectroscopy. J Biol Chem 2003, 278 : 30098 30105
    • (2003) J Biol Chem , vol.278 , pp. 30098-30105
    • Liang, Y.1    Du, F.2    Sanglier, S.3    Zhou, B.R.4    Xia, Y.5    Va Dorsselaer, N.A.6    Maechling, C.7
  • 10
    • 0031672564 scopus 로고    scopus 로고
    • Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies
    • Fan YX, Zhou JM, Kihara H, Tsou CL. Unfolding and refolding of dimeric creatine kinase equilibrium and kinetic studies. Protein Sci 1998, 7 : 2631 2641
    • (1998) Protein Sci , vol.7 , pp. 2631-2641
    • Fan, Y.X.1    Zhou, J.M.2    Kihara, H.3    Tsou, C.L.4
  • 11
    • 11144277877 scopus 로고    scopus 로고
    • Direct observation of the enthalpy change accompanying the native to molten-globule transition of cytochrome c by using isothermal acid-titration calorimetry
    • Nakamura S, Kidokoro S. Direct observation of the enthalpy change accompanying the native to molten-globule transition of cytochrome c by using isothermal acid-titration calorimetry. Biophys Chem 2005, 113 : 161 168
    • (2005) Biophys Chem , vol.113 , pp. 161-168
    • Nakamura, S.1    Kidokoro, S.2
  • 12
    • 33751418948 scopus 로고    scopus 로고
    • Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability
    • Luke K, Wittung-Stafshede P. Folding and assembly pathways of co-chaperonin proteins 10: Origin of bacterial thermostability. Arch Biochem Biophys 2006, 456 : 8 18
    • (2006) Arch Biochem Biophys , vol.456 , pp. 8-18
    • Luke, K.1    Wittung-Stafshede, P.2
  • 13
    • 33748286734 scopus 로고    scopus 로고
    • Oleic acid inhibits amyloid formation of the intermediate of α-lactalbumin at moderately acidic pH
    • Yang F Jr., Zhang M, Zhou BR, Chen J, Liang Y. Oleic acid inhibits amyloid formation of the intermediate of α-lactalbumin at moderately acidic pH. J Mol Biol 2006, 362 : 821 834
    • (2006) J Mol Biol , vol.362 , pp. 821-834
    • Yang Jr., F.1    Zhang, M.2    Zhou, B.R.3    Chen, J.4    Liang, Y.5
  • 14
    • 11244309572 scopus 로고    scopus 로고
    • Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry
    • Kardos J, Yamamoto K, Hasegawa K, Naiki H, Goto Y. Direct measurement of the thermodynamic parameters of amyloid formation by isothermal titration calorimetry. J Biol Chem 2004, 279 : 55308 55314
    • (2004) J Biol Chem , vol.279 , pp. 55308-55314
    • Kardos, J.1    Yamamoto, K.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 15
    • 11244296161 scopus 로고    scopus 로고
    • Mixed macromolecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme: Implications for protein folding in intracellular environments
    • Zhou BR, Liang Y, Du F, Zhou Z, Chen J. Mixed macromolecular crowding accelerates the oxidative refolding of reduced, denatured lysozyme: implications for protein folding in intracellular environments. J Biol Chem 2004, 279 : 55109 55116
    • (2004) J Biol Chem , vol.279 , pp. 55109-55116
    • Zhou, B.R.1    Liang, Y.2    Du, F.3    Zhou, Z.4    Chen, J.5
  • 16
    • 33750806263 scopus 로고    scopus 로고
    • Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: Implications for protein folding in physiological environments
    • Du F, Zhou Z, Mo ZY, Shi JZ, Chen J, Liang Y. Mixed macromolecular crowding accelerates the refolding of rabbit muscle creatine kinase: implications for protein folding in physiological environments. J Mol Biol 2006, 364 : 469 482
    • (2006) J Mol Biol , vol.364 , pp. 469-482
    • Du, F.1    Zhou, Z.2    Mo, Z.Y.3    Shi, J.Z.4    Chen, J.5    Liang, Y.6
  • 17
    • 43049096368 scopus 로고    scopus 로고
    • Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme
    • Zhou BR, Zhou Z, Hu QL, Chen J, Liang Y. Mixed macromolecular crowding inhibits amyloid formation of hen egg white lysozyme. Biochim Biophys Acta 2008, 1784 : 472 480
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 472-480
    • Zhou, B.R.1    Zhou, Z.2    Hu, Q.L.3    Chen, J.4    Liang, Y.5
  • 18
    • 33751115774 scopus 로고    scopus 로고
    • Fibrillogenic and non-fibrillogenic ensembles of SDS-bound human α-synuclein
    • Ahmad MF, Ramakrishna T, Raman B, Rao Ch M. Fibrillogenic and non-fibrillogenic ensembles of SDS-bound human α-synuclein. J Mol Biol 2006, 364 : 1061 1072
    • (2006) J Mol Biol , vol.364 , pp. 1061-1072
    • Ahmad, M.F.1    Ramakrishna, T.2    Raman, B.3    Rao, C.M.4
  • 20
    • 33748665734 scopus 로고    scopus 로고
    • Macromolecular crowding enhances the binding of superoxide dismutase to xanthine oxidase: Implications for protein-protein interactions in intracellular environments
    • Zhou YL, Liao JM, Chen J, Liang Y. Macromolecular crowding enhances the binding of superoxide dismutase to xanthine oxidase: implications for protein-protein interactions in intracellular environments. Int J Biochem Cell Biol 2006, 38 : 1986 1994
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 1986-1994
    • Zhou, Y.L.1    Liao, J.M.2    Chen, J.3    Liang, Y.4
  • 21
    • 12344324721 scopus 로고    scopus 로고
    • Thermodynamics of the interaction of xanthine oxidase with superoxide dismutase by isothermal titration calorimetry and fluorescence spectroscopy
    • Zhou YL, Liao JM, Chen J, Liang Y. Thermodynamics of the interaction of xanthine oxidase with superoxide dismutase by isothermal titration calorimetry and fluorescence spectroscopy. Thermochim Acta 2005, 426 : 173 178
    • (2005) Thermochim Acta , vol.426 , pp. 173-178
    • Zhou, Y.L.1    Liao, J.M.2    Chen, J.3    Liang, Y.4
  • 22
    • 33845871995 scopus 로고    scopus 로고
    • Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity
    • Jin R, Rummel A, Binz T, Brunger AT. Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 2006, 444 : 1092 1095
    • (2006) Nature , vol.444 , pp. 1092-1095
    • Jin, R.1    Rummel, A.2    Binz, T.3    Brunger, A.T.4
  • 23
    • 34250013122 scopus 로고    scopus 로고
    • Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation
    • Knipscheer P, van Dijk WJ, Olsen JV, Mann M, Sixma TK. Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. EMBO J 2007, 26 : 2797 2807
    • (2007) EMBO J , vol.26 , pp. 2797-2807
    • Knipscheer, P.1    Van Dijk, W.J.2    Olsen, J.V.3    Mann, M.4    Sixma, T.K.5
  • 24
    • 34249876632 scopus 로고    scopus 로고
    • Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40
    • Chen Y, Xu Y, Bao Q, Xing Y, Li Z, Lin Z, Stock JB et al. Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40. Nat Struct Mol Biol 2007, 14 : 527 534
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 527-534
    • Chen, Y.1    Xu, Y.2    Bao, Q.3    Xing, Y.4    Li, Z.5    Lin, Z.6    Stock, J.B.7
  • 25
    • 34250379587 scopus 로고    scopus 로고
    • Calcium-dependent and -independent binding of soybean calmodulin isoforms to the calmodulin binding domain of tobacco MAPK phosphatase-1
    • Rainaldi M, Yamniuk AP, Murase T, Vogel HJ. Calcium-dependent and -independent binding of soybean calmodulin isoforms to the calmodulin binding domain of tobacco MAPK phosphatase-1. J Biol Chem 2007, 282 : 6031 6042
    • (2007) J Biol Chem , vol.282 , pp. 6031-6042
    • Rainaldi, M.1    Yamniuk, A.P.2    Murase, T.3    Vogel, H.J.4
  • 26
    • 3042594710 scopus 로고    scopus 로고
    • Electrostatically optimized Ras-binding Ral guanine dissociation stimulator mutants increase the rate of association by stabilizing the encounter complex
    • Kiel C, Selzer T, Shaul Y, Schreiber G, Herrmann C. Electrostatically optimized Ras-binding Ral guanine dissociation stimulator mutants increase the rate of association by stabilizing the encounter complex. Proc Natl Acad Sci U S A 2004, 101 : 9223 9228
    • (2004) Proc Natl Acad Sci U S a , vol.101 , pp. 9223-9228
    • Kiel, C.1    Selzer, T.2    Shaul, Y.3    Schreiber, G.4    Herrmann, C.5
  • 27
  • 28
    • 0038813750 scopus 로고    scopus 로고
    • The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. the HyHEL-10-HEL interaction
    • Yokota A, Tsumoto K, Shiroishi M, Kondo H, Kumagai I. The role of hydrogen bonding via interfacial water molecules in antigen-antibody complexation. The HyHEL-10-HEL interaction. J Biol Chem 2003, 278 : 5410 5418
    • (2003) J Biol Chem , vol.278 , pp. 5410-5418
    • Yokota, A.1    Tsumoto, K.2    Shiroishi, M.3    Kondo, H.4    Kumagai, I.5
  • 30
    • 33745176269 scopus 로고    scopus 로고
    • Thermodynamic characterization of binding Oxytricha nova single strand telomere DNA with the alpha protein N-terminal domain
    • Buczek P, Horvath MP. Thermodynamic characterization of binding Oxytricha nova single strand telomere DNA with the alpha protein N-terminal domain. J Mol Biol 2006, 359 : 1217 1234
    • (2006) J Mol Biol , vol.359 , pp. 1217-1234
    • Buczek, P.1    Horvath, M.P.2
  • 31
    • 34447323868 scopus 로고    scopus 로고
    • High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA
    • Ziegler A, Seelig J. High affinity of the cell-penetrating peptide HIV-1 Tat-PTD for DNA. Biochemistry 2007, 46 : 8138 8145
    • (2007) Biochemistry , vol.46 , pp. 8138-8145
    • Ziegler, A.1    Seelig, J.2
  • 32
    • 34547891497 scopus 로고    scopus 로고
    • Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: Implications for the processivity mechanism
    • Loregian A, Sinigalia E, Mercorelli B, Palù G, Coen DM. Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism. Nucleic Acids Res 2007, 35 : 4779 4791
    • (2007) Nucleic Acids Res , vol.35 , pp. 4779-4791
    • Loregian, A.1    Sinigalia, E.2    Mercorelli, B.3    Palù, G.4    Coen, D.M.5
  • 33
    • 7444239630 scopus 로고    scopus 로고
    • RNA tertiary structure and cooperative assembly of a large ribonucleoprotein complex
    • Recht MI, Williamson JR. RNA tertiary structure and cooperative assembly of a large ribonucleoprotein complex. J Mol Biol 2004, 344 : 395 407
    • (2004) J Mol Biol , vol.344 , pp. 395-407
    • Recht, M.I.1    Williamson, J.R.2
  • 34
    • 14844355725 scopus 로고    scopus 로고
    • NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: Contribution of a β hairpin to RNA binding
    • Volpon L, D'Orso I, Young CR, Frasch AC, Gehring K. NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribution of a β hairpin to RNA binding. Biochemistry 2005, 44 : 3708 3717
    • (2005) Biochemistry , vol.44 , pp. 3708-3717
    • Volpon, L.1    D'Orso, I.2    Young, C.R.3    Frasch, A.C.4    Gehring, K.5
  • 35
    • 36049009770 scopus 로고    scopus 로고
    • Binding of ferulic acid to cytochrome c enhances stability of the protein at physiological pH and inhibits cytochrome c-induced apoptosis
    • Yang F, Zhou BR, Zhang P, Zhao YF, Chen J, Liang Y. Binding of ferulic acid to cytochrome c enhances stability of the protein at physiological pH and inhibits cytochrome c-induced apoptosis. Chem Biol Interact. 2007, 170 : 231 243
    • (2007) Chem Biol Interact. , vol.170 , pp. 231-243
    • Yang, F.1    Zhou, B.R.2    Zhang, P.3    Zhao, Y.F.4    Chen, J.5    Liang, Y.6
  • 36
    • 14744267536 scopus 로고    scopus 로고
    • Development of a technique to determine bicyclomycinrho binding and stoichiometry by isothermal titration calorimetry and mass spectrometry
    • Brogan AP, Widger WR, Bensadek D, Riba-Garcia I, Gaskell SJ, Kohn H. Development of a technique to determine bicyclomycinrho binding and stoichiometry by isothermal titration calorimetry and mass spectrometry. J Am Chem Soc 2005, 127 : 2741 2751
    • (2005) J Am Chem Soc , vol.127 , pp. 2741-2751
    • Brogan, A.P.1    Widger, W.R.2    Bensadek, D.3    Riba-Garcia, I.4    Gaskell, S.J.5    Kohn, H.6
  • 37
  • 38
    • 33947502906 scopus 로고    scopus 로고
    • Inhibition of metalloprotease botulinum serotype a from a pseudo-peptide binding mode to a small molecule that is active in primary neurons
    • Burnett JC, Ruthel G, Stegmann CM, Panchal RG., Nguyen TL, Hermone AR, Stafford RG et al. Inhibition of metalloprotease botulinum serotype A from a pseudo-peptide binding mode to a small molecule that is active in primary neurons. J Biol Chem 2007, 282 : 5004 5014
    • (2007) J Biol Chem , vol.282 , pp. 5004-5014
    • Burnett, J.C.1    Ruthel, G.2    Stegmann, C.M.3    Panchal, R.G.4    Nguyen, T.L.5    Hermone, A.R.6    Stafford, R.G.7
  • 39
    • 34447498409 scopus 로고    scopus 로고
    • Glyoxylate and pyruvate are antagonistic effectors of the Escherichia coli IclR transcriptional regulator
    • Lorca GL, Ezersky A, Lunin VV, Walker JR, Altamentova S, Evdokimova E, Vedadi M et al. Glyoxylate and pyruvate are antagonistic effectors of the Escherichia coli IclR transcriptional regulator. J Biol Chem 2007, 282 : 16476 16491
    • (2007) J Biol Chem , vol.282 , pp. 16476-16491
    • Lorca, G.L.1    Ezersky, A.2    Lunin, V.V.3    Walker, J.R.4    Altamentova, S.5    Evdokimova, E.6    Vedadi, M.7
  • 40
    • 39149086419 scopus 로고    scopus 로고
    • Isothermal titration calorimetry of metal ions binding to proteins: An overview of recent studies
    • Wilcox DE. Isothermal titration calorimetry of metal ions binding to proteins: an overview of recent studies. Inorganica Chim Acta 2008, 361 : 857 867
    • (2008) Inorganica Chim Acta , vol.361 , pp. 857-867
    • Wilcox, D.E.1
  • 41
    • 30044443305 scopus 로고    scopus 로고
    • High affinity binding between copper and full-length prion protein identified by two different techniques
    • Thompsett AR, Abdelraheim SR, Daniels M, Brown DR. High affinity binding between copper and full-length prion protein identified by two different techniques. J Biol Chem 2005, 280 : 42750 42758
    • (2005) J Biol Chem , vol.280 , pp. 42750-42758
    • Thompsett, A.R.1    Abdelraheim, S.R.2    Daniels, M.3    Brown, D.R.4
  • 42
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-affinity ligands
    • Velazquez-Campoy A, Freire E. Isothermal titration calorimetry to determine association constants for high-affinity ligands. Nat Protoc 2006, 1 : 186 191
    • (2006) Nat Protoc , vol.1 , pp. 186-191
    • Velazquez-Campoy, A.1    Freire, E.2
  • 43
    • 39649115803 scopus 로고    scopus 로고
    • Formation of a wrapped DNA-protein interface: Experimental characterization and analysis of the large contributions of ions and water to the thermodynamics of binding IHF to H' DNA
    • Vander Meulen KA, Saecker RM, Record MT Jr. Formation of a wrapped DNA-protein interface: experimental characterization and analysis of the large contributions of ions and water to the thermodynamics of binding IHF to H' DNA. J Mol Biol 2008, 377 : 9 27
    • (2008) J Mol Biol , vol.377 , pp. 9-27
    • Ka, V.M.1    Saecker, R.M.2    Record Jr., M.T.3
  • 45
    • 14744271960 scopus 로고    scopus 로고
    • ITC in the post-genomic era Priceless
    • Velázquez Campoy A, Freire E. ITC in the post-genomic era Priceless. Biophys Chem 2005, 115 : 115 124
    • (2005) Biophys Chem , vol.115 , pp. 115-124
    • Velázquez, C.A.1    Freire, E.2
  • 46
    • 34447283577 scopus 로고    scopus 로고
    • Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method
    • Andújar-Sánchez M, Jara-Pérez V, Cámara-Artigas A. Thermodynamic determination of the binding constants of angiotensin-converting enzyme inhibitors by a displacement method. FEBS Lett 2007, 581 : 3449 3454
    • (2007) FEBS Lett , vol.581 , pp. 3449-3454
    • Andújar-Sánchez, M.1    Jara-Pérez, V.2    Cámara-Artigas, A.3


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