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Volumn , Issue , 2013, Pages 139-177

Calorimetric Methods to Characterize the Forces Driving Macromolecular Association and Folding Processes

Author keywords

Differential scanning calorimetry (DSC); Isothermal titration calorimetry (ITC); Macromolecular association; Macromolecular folding processes; Proteins; Thermodynamic properties

Indexed keywords


EID: 84886346877     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781118523063.ch7     Document Type: Chapter
Times cited : (4)

References (192)
  • 1
    • 48249102785 scopus 로고    scopus 로고
    • Calorimetry and thermodynamics in drug design
    • Chaires JB. Calorimetry and thermodynamics in drug design. Annu Rev Biophys 2008;37:135-151
    • (2008) Annu Rev Biophys , vol.37 , pp. 135-151
    • Chaires, J.B.1
  • 2
    • 0035806423 scopus 로고    scopus 로고
    • Structure-based drug design
    • Henry C. Structure-based drug design. Chem Eng News 2001;79:69-74
    • (2001) Chem Eng News , vol.79 , pp. 69-74
    • Henry, C.1
  • 4
    • 0034984729 scopus 로고    scopus 로고
    • Calorimetric analyses of hyperthermophile proteins
    • In:, Michael WW, Adams RMK, editors, San Diego, CA:Academic Press
    • Shriver JW, Peters WB, Szary N, Clark AT, Edmondson SP. Calorimetric analyses of hyperthermophile proteins. In:Michael WW, Adams RMK, editors. Methods in Enzymology. San Diego, CA:Academic Press; 2001. p 389-422.
    • (2001) Methods in Enzymology , pp. 389-422
    • Shriver, J.W.1    Peters, W.B.2    Szary, N.3    Clark, A.T.4    Edmondson, S.P.5
  • 5
    • 84886331694 scopus 로고    scopus 로고
    • Thermodynamics and Kinetics of Nucleic Acid Association/Dissociation and Folding Processes
    • Oxford, UK: Elsevier Science
    • Plum G, Breslauer K, Roberts R. Thermodynamics and Kinetics of Nucleic Acid Association/Dissociation and Folding Processes. Volume 7. Oxford, UK:Elsevier Science; 1999.
    • (1999) , vol.7
    • Plum, G.1    Breslauer, K.2    Roberts, R.3
  • 6
    • 0028098629 scopus 로고
    • Introduction to microcalorimetry and biomolecular energetics
    • Cooper A, Johnson C. Introduction to microcalorimetry and biomolecular energetics. Methods Mol Biol 1994;22:109-124
    • (1994) Methods Mol Biol , vol.22 , pp. 109-124
    • Cooper, A.1    Johnson, C.2
  • 7
    • 33846637900 scopus 로고    scopus 로고
    • Microcalorimetry of biological macromolecules
    • Privalov PL, Dragan AI. Microcalorimetry of biological macromolecules. Biophys Chem 2007;126:16-24
    • (2007) Biophys Chem , vol.126 , pp. 16-24
    • Privalov, P.L.1    Dragan, A.I.2
  • 8
    • 0029064484 scopus 로고
    • Significant discrepancies between van't Hoff and calorimetric enthalpies
    • Naghibi, H, Tamura, A, Sturtevant JM. Significant discrepancies between van't Hoff and calorimetric enthalpies. Proc Natl Acad Sci USA 1995;92:5597.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5597
    • Naghibi, H.1    Tamura, A.2    Sturtevant, J.M.3
  • 9
    • 0037310209 scopus 로고    scopus 로고
    • Applications of calorimetric methods to drug discovery and the study of protein interactions
    • Weber, P, Salemme, F. Applications of calorimetric methods to drug discovery and the study of protein interactions. Curr Opin Struct Biol 2003;13:115-221
    • (2003) Curr Opin Struct Biol , vol.13 , pp. 115-221
    • Weber, P.1    Salemme, F.2
  • 10
    • 74149083849 scopus 로고    scopus 로고
    • Innovation adding calorimetric data to decision making in lead discovery:a hot tip
    • Ladbury JE, Klebe G, Freire E. Innovation adding calorimetric data to decision making in lead discovery:a hot tip. Nat Rev Drug Discov 2010;9:23-27
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 23-27
    • Ladbury, J.E.1    Klebe, G.2    Freire, E.3
  • 11
    • 77955971738 scopus 로고    scopus 로고
    • Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design
    • Ladbury JE. Calorimetry as a tool for understanding biomolecular interactions and an aid to drug design. Biochem Soc Trans 2010;38:888-893
    • (2010) Biochem Soc Trans , vol.38 , pp. 888-893
    • Ladbury, J.E.1
  • 12
    • 70349731747 scopus 로고    scopus 로고
    • A thermodynamic approach to the affinity optimization of drug candidates
    • Freire E. A thermodynamic approach to the affinity optimization of drug candidates. Chem Biol Drug Des 2009;74:468-472
    • (2009) Chem Biol Drug Des , vol.74 , pp. 468-472
    • Freire, E.1
  • 13
    • 52049123291 scopus 로고    scopus 로고
    • Do enthalpy and entropy distinguish first in class from best in class?
    • Freire, E. Do enthalpy and entropy distinguish first in class from best in class? Drug Discov Today 2008;13:869-874.
    • (2008) Drug Discov Today , vol.13 , pp. 869-874
    • Freire, E.1
  • 14
    • 0003491401 scopus 로고
    • Analytical solution calorimetry
    • In:, Elving PJ, Winefordner JD, Kolthoff IM, editors, New York:John Wiley
    • Grime JK. Analytical solution calorimetry. In:Elving PJ, Winefordner JD, Kolthoff IM, editors. Chemical Analysis. New York:John Wiley; 1985.
    • (1985) Chemical Analysis
    • Grime, J.K.1
  • 15
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T,Williston S, Brandts JF, Lin LN. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal Biochem 1989;179:131-137
    • (1989) Anal Biochem , vol.179 , pp. 131-137
    • Wiseman, T.1    Williston, S.2    Brandts, J.F.3    Lin, L.N.4
  • 16
    • 0026687954 scopus 로고
    • Calorimetry -a tool for DNA and ligand-DNA studies
    • Breslauer KJ, Freire E, Straume M. Calorimetry -a tool for DNA and ligand-DNA studies. Methods Enzymol 1992;211:533-567
    • (1992) Methods Enzymol , vol.211 , pp. 533-567
    • Breslauer, K.J.1    Freire, E.2    Straume, M.3
  • 17
    • 0036684445 scopus 로고    scopus 로고
    • Thermal denaturation of influenza virus and its relationship to membrane fusion
    • Epand RM, Epand RF. Thermal denaturation of influenza virus and its relationship to membrane fusion. Biochem J 2002;365:841-848
    • (2002) Biochem J , vol.365 , pp. 841-848
    • Epand, R.M.1    Epand, R.F.2
  • 19
    • 0030971891 scopus 로고    scopus 로고
    • Possible origin of differences between van't Hoff and calorimetric enthalpy estimates
    • Chaires JB. Possible origin of differences between van't Hoff and calorimetric enthalpy estimates. Biophys Chem 1997;64:15-23
    • (1997) Biophys Chem , vol.64 , pp. 15-23
    • Chaires, J.B.1
  • 20
    • 0035852865 scopus 로고    scopus 로고
    • van't Hoff and calorimetric enthalpies from isothermal titration calorimetry:are there significant discrepancies?
    • Horn JR, Russell D, Lewis EA, Murphy KP. van't Hoff and calorimetric enthalpies from isothermal titration calorimetry:are there significant discrepancies? Biochemistry 2001;40:1774-1778.
    • (2001) Biochemistry , vol.40 , pp. 1774-1778
    • Horn, J.R.1    Russell, D.2    Lewis, E.A.3    Murphy, K.P.4
  • 21
    • 0037062633 scopus 로고    scopus 로고
    • van't Hoff and calorimetric enthalpies II:effects of linked equilibria
    • Horn JR, Brandts JF, Murphy KP. van't Hoff and calorimetric enthalpies II:effects of linked equilibria. Biochemistry 2002;41:7501-7507
    • (2002) Biochemistry , vol.41 , pp. 7501-7507
    • Horn, J.R.1    Brandts, J.F.2    Murphy, K.P.3
  • 22
  • 23
    • 84891585273 scopus 로고    scopus 로고
    • Microcalorimetry of macromolecules:the physical basis of biological structures
    • New York:John Wiley
    • Privalov PL. Microcalorimetry of macromolecules:the physical basis of biological structures. Wiley Series in Protein and Peptide Science. New York:John Wiley; 2012.
    • (2012) Wiley Series in Protein and Peptide Science
    • Privalov, P.L.1
  • 24
    • 84886335966 scopus 로고    scopus 로고
    • Microcalorimetry of proteins and their complexes
    • In:Shriver JW, editor. Protein Structure, Stability, and Interactions. Totowa, NJ:The Humana Press
    • Privalov PL. Microcalorimetry of proteins and their complexes. In:Shriver JW, editor. Protein Structure, Stability, and Interactions. Totowa, NJ:The Humana Press; 2008. p 1-39.
    • (2008)
    • Privalov, P.L.1
  • 25
  • 26
    • 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
  • 27
    • 37549057040 scopus 로고    scopus 로고
    • Applications of isothermal titration calorimetry in RNA biochemistry and biophysics
    • Feig AL. Applications of isothermal titration calorimetry in RNA biochemistry and biophysics. Biopolymers 2007;87:293-301
    • (2007) Biopolymers , vol.87 , pp. 293-301
    • Feig, A.L.1
  • 28
    • 3543005385 scopus 로고    scopus 로고
    • Thermodynamics of protein-ligand interactions:history, presence, and future aspects
    • Perozzo R, Folkers G, Scapozza L. Thermodynamics of protein-ligand interactions:history, presence, and future aspects. J Recept Signal Transduct 2004;24:1-52
    • (2004) J Recept Signal Transduct , vol.24 , pp. 1-52
    • Perozzo, R.1    Folkers, G.2    Scapozza, L.3
  • 29
    • 0042831474 scopus 로고    scopus 로고
    • A study of statistical error in isothermal titration calorimetry
    • Tellinghuisen J. A study of statistical error in isothermal titration calorimetry. Anal Biochem 2003;321:79-88
    • (2003) Anal Biochem , vol.321 , pp. 79-88
    • Tellinghuisen, J.1
  • 30
    • 1642546385 scopus 로고    scopus 로고
    • Statistical error in isothermal titration calorimetry
    • In:Ludwig B, Michael LJ, editors, San Diego, CA:Academic Press
    • Tellinghuisen J. Statistical error in isothermal titration calorimetry. In:Ludwig B, Michael LJ, editors. Methods in Enzymology. San Diego, CA:Academic Press; 2004. p 245-282.
    • (2004) Methods in Enzymology
    • Tellinghuisen, J.1
  • 31
    • 22144459822 scopus 로고    scopus 로고
    • Statistical error in isothermal titration calorimetry:variance function estimation from generalized least squares
    • Tellinghuisen J. Statistical error in isothermal titration calorimetry:variance function estimation from generalized least squares. Anal Biochem 2005;343:106-115
    • (2005) Anal Biochem , vol.343 , pp. 106-115
    • Tellinghuisen, J.1
  • 32
    • 33845437051 scopus 로고    scopus 로고
    • Calibration in isothermal titration calorimetry:heat and cell volume from heat of dilution of NaCl(aq)
    • Tellinghuisen J. Calibration in isothermal titration calorimetry:heat and cell volume from heat of dilution of NaCl(aq). Anal Biochem 2007;360:47-55
    • (2007) Anal Biochem , vol.360 , pp. 47-55
    • Tellinghuisen, J.1
  • 33
    • 37549033509 scopus 로고    scopus 로고
    • Isothermal titration calorimetry at very low c
    • Tellinghuisen J. Isothermal titration calorimetry at very low c. Anal Biochem 2008;373:395-397
    • (2008) Anal Biochem , vol.373 , pp. 395-397
    • Tellinghuisen, J.1
  • 34
    • 78650943856 scopus 로고    scopus 로고
    • Thermodynamic dissection of colicin interactions
    • In:Michael L, Johnson JMH, Gary KA, editors, San Diego, CA:Academic Press
    • Housden NG, Kleanthous C. Thermodynamic dissection of colicin interactions. In:Michael L, Johnson JMH, Gary KA, editors. Methods in Enzymology. San Diego, CA:Academic Press; 2011. p 123-145.
    • (2011) Methods in Enzymology , pp. 123-145
    • Housden, N.G.1    Kleanthous, C.2
  • 35
    • 38449103279 scopus 로고    scopus 로고
    • Biophysical and biochemical investigations of dsRNA-activated kinase PKR
    • In:Jon L, editor, San Diego, CA:Academic Press
    • McKenna SA, Lindhout DA, Shimoike T, Puglisi JD. Biophysical and biochemical investigations of dsRNA-activated kinase PKR. In:Jon L, editor. Methods in Enzymology. San Diego, CA:Academic Press; 2007. p 373-396.
    • (2007) Methods in Enzymology , pp. 373-396
    • McKenna, S.A.1    Lindhout, D.A.2    Shimoike, T.3    Puglisi, J.D.4
  • 36
    • 0034650726 scopus 로고    scopus 로고
    • Exact analysis of competition ligand binding by displacement isothermal titration calorimetry
    • Sigurskjold BW. Exact analysis of competition ligand binding by displacement isothermal titration calorimetry. Anal Biochem 2000;277:260-266
    • (2000) Anal Biochem , vol.277 , pp. 260-266
    • Sigurskjold, B.W.1
  • 38
    • 61849154739 scopus 로고    scopus 로고
    • Characterization of parvalbumin and polcalcin divalent ion binding by isothermal titration calorimetry
    • In:, Part A. San Diego:Elsevier Academic Press
    • Henzl MT. Characterization of parvalbumin and polcalcin divalent ion binding by isothermal titration calorimetry. In:Methods in Enzymology:Biothermodynamics, Volume 455:Part A. San Diego:Elsevier Academic Press; 2009. p 259-297.
    • (2009) Methods in Enzymology:Biothermodynamics , vol.455 , pp. 259-297
    • Henzl, M.T.1
  • 40
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • Brandts JF, Lin LN. Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 1990;29:6927-6940
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.N.2
  • 41
    • 0033544727 scopus 로고    scopus 로고
    • The energetics of HMG box interactions with DNA:thermodynamics of the DNA binding of the HMG box from mouse Sox-5
    • Privalov PL, Jelesarov I, Read CM, Dragan AI, Crane-Robinson C. The energetics of HMG box interactions with DNA:thermodynamics of the DNA binding of the HMG box from mouse Sox-5. J Mol Biol 1999;294:997-1013
    • (1999) J Mol Biol , vol.294 , pp. 997-1013
    • Privalov, P.L.1    Jelesarov, I.2    Read, C.M.3    Dragan, A.I.4    Crane-Robinson, C.5
  • 42
    • 0042166066 scopus 로고    scopus 로고
    • DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial nonelectrostatic contribution
    • Dragan AI, Klass J, Read C, Churchill MEA, Crane-Robinson C, Privalov PL. DNA binding of a non-sequence-specific HMG-D protein is entropy driven with a substantial nonelectrostatic contribution. J Mol Biol 2003;331:795-813
    • (2003) J Mol Biol , vol.331 , pp. 795-813
    • Dragan, A.I.1    Klass, J.2    Read, C.3    Churchill, M.E.A.4    Crane-Robinson, C.5    Privalov, P.L.6
  • 44
    • 61849095281 scopus 로고    scopus 로고
    • Isothermal titration calorimetry:general formalism using binding polynomials
    • In:Michael L, Johnson JMH, Gary KA, editors, San Diego, CA:Academic Press
    • Freire E, Schön A, VelazquezCampoy A. Isothermal titration calorimetry:general formalism using binding polynomials. In:Michael L, Johnson JMH, Gary KA, editors. Methods in Enzymology. San Diego, CA:Academic Press; 2009. p 127-155.
    • (2009) Methods in Enzymology , pp. 127-155
    • Freire, E.1    Schön, A.2    VelazquezCampoy, A.3
  • 45
    • 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 1991;192:203-206
    • (1991) Anal Biochem , vol.192 , pp. 203-206
    • Bains, G.1    Freire, E.2
  • 46
    • 0033544722 scopus 로고    scopus 로고
    • The energetics ofHMGbox interactions with DNA:thermodynamic description of the target DNA duplexes
    • Jelesarov I, Crane-Robinson C, Privalov PL. The energetics ofHMGbox interactions with DNA:thermodynamic description of the target DNA duplexes. J Mol Biol 1999;294:981-995
    • (1999) J Mol Biol , vol.294 , pp. 981-995
    • Jelesarov, I.1    Crane-Robinson, C.2    Privalov, P.L.3
  • 47
    • 0034581192 scopus 로고    scopus 로고
    • Problems and prospects in microcalorimetry of biological macromolecules
    • In:Michael L, Johnson GKA, editors, San Diego, CA:Academic Press
    • Privalov GP, Privalov PL. Problems and prospects in microcalorimetry of biological macromolecules. In:Michael L, Johnson GKA, editors. Methods in Enzymology. San Diego, CA:Academic Press; 2000. p 31-62.
    • (2000) Methods in Enzymology , pp. 31-62
    • Privalov, G.P.1    Privalov, P.L.2
  • 48
    • 0017895903 scopus 로고
    • The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides
    • Manning GS. The molecular theory of polyelectrolyte solutions with applications to the electrostatic properties of polynucleotides. Q Rev Biophys 1978;11:179-246
    • (1978) Q Rev Biophys , vol.11 , pp. 179-246
    • Manning, G.S.1
  • 49
    • 0017820499 scopus 로고
    • Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids:the roles of ion association or release, screening, and ion effects on water activity
    • Record M, Anderson C. Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids:the roles of ion association or release, screening, and ion effects on water activity. Q Rev Biophys 1978;11:103-178
    • (1978) Q Rev Biophys , vol.11 , pp. 103-178
    • Record, M.1    Anderson, C.2
  • 50
    • 0025264701 scopus 로고
    • Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids
    • Mascotti DP, Lohman TM. Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids. Proc Natl Acad Sci U S A 1990;87:3142-3146
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 3142-3146
    • Mascotti, D.P.1    Lohman, T.M.2
  • 51
    • 79954618050 scopus 로고    scopus 로고
    • Interpreting protein/DNA interactions:distinguishing specific from nonspecific and electrostatic from non-electrostatic components
    • Privalov PL, Dragan AI, Crane-Robinson C. Interpreting protein/DNA interactions:distinguishing specific from nonspecific and electrostatic from non-electrostatic components. Nucleic Acids Res 2011;39(7):2483-2491.
    • (2011) Nucleic Acids Res , vol.39 , Issue.7 , pp. 2483-2491
    • Privalov, P.L.1    Dragan, A.I.2    Crane-Robinson, C.3
  • 53
    • 27444436325 scopus 로고    scopus 로고
    • Stability and DNA binding ability of the DNA binding domains of interferon regulatory factors 1 and 3
    • Hargreaves VV, Makeyeva EN, Dragan AI, Privalov PL. Stability and DNA binding ability of the DNA binding domains of interferon regulatory factors 1 and 3. Biochemistry 2005;44:14202-14209
    • (2005) Biochemistry , vol.44 , pp. 14202-14209
    • Hargreaves, V.V.1    Makeyeva, E.N.2    Dragan, A.I.3    Privalov, P.L.4
  • 54
    • 5144227739 scopus 로고    scopus 로고
    • Thermodynamic signature of GCN4-bZIP binding to DNA indicates the role of water in discriminating between the AP-1 and ATF/CREB sites
    • Dragan AI, Frank L, Liu YY, Makeyeva EN, Crane-Robinson C, Privalov PL. Thermodynamic signature of GCN4-bZIP binding to DNA indicates the role of water in discriminating between the AP-1 and ATF/CREB sites. J Mol Biol 2004;343:865-878
    • (2004) J Mol Biol , vol.343 , pp. 865-878
    • Dragan, A.I.1    Frank, L.2    Liu, Y.Y.3    Makeyeva, E.N.4    Crane-Robinson, C.5    Privalov, P.L.6
  • 56
    • 0037459241 scopus 로고    scopus 로고
    • The energetics of specific binding of AT-hooks from HMGA1 to target DNA
    • Dragan AI, Liggins JR, Crane-Robinson C, Privalov PL. The energetics of specific binding of AT-hooks from HMGA1 to target DNA. J Mol Biol 2003;327:393-411
    • (2003) J Mol Biol , vol.327 , pp. 393-411
    • Dragan, A.I.1    Liggins, J.R.2    Crane-Robinson, C.3    Privalov, P.L.4
  • 57
    • 0028887796 scopus 로고
    • Grand canonical Monte Carlo molecular and thermodynamic predictions of ion effects on binding of an oligocation (l8+) to the center of DNA oligomers
    • Olmsted MC, Bond JP, Anderson CF, Record Jr M. Grand canonical Monte Carlo molecular and thermodynamic predictions of ion effects on binding of an oligocation (l8+) to the center of DNA oligomers. Biophys J 1995;68:634-647
    • (1995) Biophys J , vol.68 , pp. 634-647
    • Olmsted, M.C.1    Bond, J.P.2    Anderson, C.F.3    Record Jr, M.4
  • 58
    • 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
  • 59
    • 0035981605 scopus 로고    scopus 로고
    • Thermodynamic quantities for the ionization reactions of buffers
    • Goldberg RN, Kishore N, Lennen RM. Thermodynamic quantities for the ionization reactions of buffers. J Phys Chem Ref Data 2002;31:231-370
    • (2002) J Phys Chem Ref Data , vol.31 , pp. 231-370
    • Goldberg, R.N.1    Kishore, N.2    Lennen, R.M.3
  • 60
    • 0023668218 scopus 로고
    • Differential scanning calorimetric study of the thermal unfolding of Taka-amylase A from Aspergillus oryzae
    • Fukada H, Takahashi K, Sturtevant JM. Differential scanning calorimetric study of the thermal unfolding of Taka-amylase A from Aspergillus oryzae. Biochemistry 1987;26:4063-4068
    • (1987) Biochemistry , vol.26 , pp. 4063-4068
    • Fukada, H.1    Takahashi, K.2    Sturtevant, J.M.3
  • 61
    • 0031670461 scopus 로고    scopus 로고
    • Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 Mpotassium chloride
    • Fukada H, Takahashi K. Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 Mpotassium chloride. Prot Struct Funct Genet 1998;33:159-166
    • (1998) Prot Struct Funct Genet , vol.33 , pp. 159-166
    • Fukada, H.1    Takahashi, K.2
  • 62
    • 0003935008 scopus 로고
    • Handbook of Proton Ionization Heats and Related Thermodynamic Quantities
    • New York:John Wiley
    • Christensen JJ, Hansen LD, Izatt RM. Handbook of Proton Ionization Heats and Related Thermodynamic Quantities. New York:John Wiley; 1976.
    • (1976)
    • Christensen, J.J.1    Hansen, L.D.2    Izatt, R.M.3
  • 63
    • 84863052766 scopus 로고    scopus 로고
    • Thermodynamics of coupled folding in the interaction of archaeal RNase P proteins RPP21 and RPP29
    • Xu Y, Oruganti SV, Gopalan V, Foster MP. Thermodynamics of coupled folding in the interaction of archaeal RNase P proteins RPP21 and RPP29. Biochemistry 2011;51:926-935
    • (2011) Biochemistry , vol.51 , pp. 926-935
    • Xu, Y.1    Oruganti, S.V.2    Gopalan, V.3    Foster, M.P.4
  • 64
    • 0026684671 scopus 로고
    • Use of liquidhydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar RS, Livingstone JR, Record MT. Use of liquidhydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry 1992;31:3947-3955
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record, M.T.3
  • 65
    • 23444450909 scopus 로고
    • Coupling of local folding to sitespecific binding of proteins to DNA
    • Spolar RS, Record MT. Coupling of local folding to sitespecific binding of proteins to DNA. Science 1994;263:777-784
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 66
    • 77449114899 scopus 로고    scopus 로고
    • Stability and DNAbinding ability of the bZIP dimers formed by the ATF-2 and c-Jun transcription factors
    • Carrillo RJ, Dragan AI, Privalov PL. Stability and DNAbinding ability of the bZIP dimers formed by the ATF-2 and c-Jun transcription factors. J Mol Biol 2010;396:431-440
    • (2010) J Mol Biol , vol.396 , pp. 431-440
    • Carrillo, R.J.1    Dragan, A.I.2    Privalov, P.L.3
  • 67
    • 84886333674 scopus 로고    scopus 로고
    • Biot 297 -stability of the bZIP homo-and heterodimers and energetics of their interactions with DNA
    • Carrillo R, Dragan AI, Privalov PL. Biot 297 -stability of the bZIP homo-and heterodimers and energetics of their interactions with DNA. Abstr Pap Am Chem Soc 2007;234.
    • (2007) Abstr Pap Am Chem Soc , pp. 234
    • Carrillo, R.1    Dragan, A.I.2    Privalov, P.L.3
  • 69
    • 0031016315 scopus 로고    scopus 로고
    • Energetics of folding and DNA binding of the MAT alpha 2 homeodomain
    • Carra JH, Privalov PL. Energetics of folding and DNA binding of the MAT alpha 2 homeodomain. Biochemistry 1997;36:526-535
    • (1997) Biochemistry , vol.36 , pp. 526-535
    • Carra, J.H.1    Privalov, P.L.2
  • 70
    • 4444231223 scopus 로고    scopus 로고
    • Structural and energetic characterization of nucleic acid-binding to the fingers domain of moloney murine leukemia virus reverse transcriptase
    • Crowther RL, Remeta DP, Minetti CASA, Das D, Montano SP, Georgiadis MM. Structural and energetic characterization of nucleic acid-binding to the fingers domain of moloney murine leukemia virus reverse transcriptase. Proteins 2004;57:15-26
    • (2004) Proteins , vol.57 , pp. 15-26
    • Crowther, R.L.1    Remeta, D.P.2    Minetti, C.A.S.A.3    Das, D.4    Montano, S.P.5    Georgiadis, M.M.6
  • 71
    • 0034435652 scopus 로고    scopus 로고
    • Structural and thermodynamic strategies for site-specific DNA binding proteins
    • Jen-Jacobson L, Engler LE, Jacobson LA. Structural and thermodynamic strategies for site-specific DNA binding proteins. Structure 2000;8:1015-1023
    • (2000) Structure , vol.8 , pp. 1015-1023
    • Jen-Jacobson, L.1    Engler, L.E.2    Jacobson, L.A.3
  • 72
    • 84886341358 scopus 로고    scopus 로고
    • Biophysics of protein-protein interactions
    • In:, Giralt E, Peczuh M, Salvatella X, editors, New York:JohnWiley
    • Luque I. Biophysics of protein-protein interactions. In:Giralt E, Peczuh M, Salvatella X, editors. Protein Surface Recognition:Approaches for Drug Discovery. New York:JohnWiley; 2011.
    • (2011) Protein Surface Recognition:Approaches for Drug Discovery
    • Luque, I.1
  • 73
    • 0036836538 scopus 로고    scopus 로고
    • Structural parameterization of the binding enthalpy of small ligands
    • Luque I, Freire E. Structural parameterization of the binding enthalpy of small ligands. Prot Struct Funct Genet 2002;49:181-190
    • (2002) Prot Struct Funct Genet , vol.49 , pp. 181-190
    • Luque, I.1    Freire, E.2
  • 74
    • 0033656239 scopus 로고    scopus 로고
    • Binding of small organic molecules to macromolecular targets:evaluation of conformational entropy changes
    • D'Aquino JA, Freire E, Amzel LM. Binding of small organic molecules to macromolecular targets:evaluation of conformational entropy changes. Prot Struct Funct Genet 2000;41:93-107
    • (2000) Prot Struct Funct Genet , vol.41 , pp. 93-107
    • D'Aquino, J.A.1    Freire, E.2    Amzel, L.M.3
  • 75
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • Kauzmann W. Some factors in the interpretation of protein denaturation. Adv Protein Chem 1959;14:1-63
    • (1959) Adv Protein Chem , vol.14 , pp. 1-63
    • Kauzmann, W.1
  • 76
    • 0030466444 scopus 로고    scopus 로고
    • Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design
    • Ladbury JE. Just add water! The effect of water on the specificity of protein-ligand binding sites and its potential application to drug design. Chem Biol 1996;3:973-980
    • (1996) Chem Biol , vol.3 , pp. 973-980
    • Ladbury, J.E.1
  • 77
    • 67650513578 scopus 로고    scopus 로고
    • Molecular dynamics of water-mediated interactions of a linear benzimidazole-biphenyl diamidine with the DNA minor groove
    • Athri P,Wilson WD. Molecular dynamics of water-mediated interactions of a linear benzimidazole-biphenyl diamidine with the DNA minor groove. J Am Chem Soc 2009;131:7618-7625
    • (2009) J Am Chem Soc , vol.131 , pp. 7618-7625
    • Athri, P.1    Wilson, W.D.2
  • 78
    • 33745032291 scopus 로고    scopus 로고
    • Water mediation in protein folding and molecular recognition
    • Levy Y, Onuchic JN. Water mediation in protein folding and molecular recognition. Annu Rev Biophys Biomol Struct 2006;35:389-415
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 389-415
    • Levy, Y.1    Onuchic, J.N.2
  • 79
    • 1842534583 scopus 로고    scopus 로고
    • MHC-peptide binding is assisted by bound water molecules
    • Petrone P, Garcia AE. MHC-peptide binding is assisted by bound water molecules. J Mol Biol 2004;338:419-435
    • (2004) J Mol Biol , vol.338 , pp. 419-435
    • Petrone, P.1    Garcia, A.E.2
  • 80
    • 0037449138 scopus 로고    scopus 로고
    • Energetics of lesion recognition by a DNA repair protein:thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA duplexes
    • Minetti CASA, Remeta DP, Zharkov DO, Plum GE, Johnson F, Grollman AP, Breslauer KJ. Energetics of lesion recognition by a DNA repair protein:thermodynamic characterization of formamidopyrimidine-glycosylase (Fpg) interactions with damaged DNA duplexes. J Mol Biol 2003;328:1047-1060
    • (2003) J Mol Biol , vol.328 , pp. 1047-1060
    • Minetti, C.A.S.A.1    Remeta, D.P.2    Zharkov, D.O.3    Plum, G.E.4    Johnson, F.5    Grollman, A.P.6    Breslauer, K.J.7
  • 83
    • 0000866128 scopus 로고
    • Hydrophobic effect in protein folding and other noncovalent processes involving proteins
    • Spolar RS, Ha JH, Record MT. Hydrophobic effect in protein folding and other noncovalent processes involving proteins. Proc Natl Acad Sci U S A 1989;86:8382-8385
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 8382-8385
    • Spolar, R.S.1    Ha, J.H.2    Record, M.T.3
  • 84
    • 0025906146 scopus 로고
    • Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface-area
    • Livingstone JR, Spolar RS, Record MT. Contribution to the thermodynamics of protein folding from the reduction in water-accessible nonpolar surface-area. Biochemistry 1991;30:4237-4244
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.R.1    Spolar, R.S.2    Record, M.T.3
  • 85
    • 78650894342 scopus 로고    scopus 로고
    • Survey of the year 2009:applications of isothermal titration calorimetry
    • Falconer RJ, Collins BM. Survey of the year 2009:applications of isothermal titration calorimetry. J Mol Recognit 2011;24:1-16
    • (2011) J Mol Recognit , vol.24 , pp. 1-16
    • Falconer, R.J.1    Collins, B.M.2
  • 86
    • 77956404669 scopus 로고    scopus 로고
    • Survey of the year 2008:applications of isothermal titration calorimetry
    • Falconer RJ, Penkova A, Jelesarov I, Collins BM. Survey of the year 2008:applications of isothermal titration calorimetry. J Mol Recognit 2010;23:395-413
    • (2010) J Mol Recognit , vol.23 , pp. 395-413
    • Falconer, R.J.1    Penkova, A.2    Jelesarov, I.3    Collins, B.M.4
  • 87
    • 34247368602 scopus 로고    scopus 로고
    • Applications of isothermal titration calorimetry in protein folding and molecular recognition
    • Liang Y. Applications of isothermal titration calorimetry in protein folding and molecular recognition. J Iran Chem Soc 2006;3:209-219
    • (2006) J Iran Chem Soc , vol.3 , pp. 209-219
    • Liang, Y.1
  • 88
    • 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
  • 90
    • 0036382925 scopus 로고    scopus 로고
    • Unfolding of a leucine zipper is not a simple two-state transition
    • Dragan AI, Privalov PL. Unfolding of a leucine zipper is not a simple two-state transition. J Mol Biol 2002;321:891-908
    • (2002) J Mol Biol , vol.321 , pp. 891-908
    • Dragan, A.I.1    Privalov, P.L.2
  • 91
    • 4944226045 scopus 로고    scopus 로고
    • DNAbinding domain of GCN4 induces bending of both the ATF/CREB and AP-1 binding sites of DNA
    • Dragan AI, Liu YY, Makeyeva EN, Privalov PL. DNAbinding domain of GCN4 induces bending of both the ATF/CREB and AP-1 binding sites of DNA. Nucleic Acids Res 2004;32:5192-5197
    • (2004) Nucleic Acids Res , vol.32 , pp. 5192-5197
    • Dragan, A.I.1    Liu, Y.Y.2    Makeyeva, E.N.3    Privalov, P.L.4
  • 97
    • 33747802145 scopus 로고    scopus 로고
    • A thermodynamic signature for drug-DNA binding mode
    • Chaires JB. A thermodynamic signature for drug-DNA binding mode. Arch Biochem Biophys 2006;453:26-31
    • (2006) Arch Biochem Biophys , vol.453 , pp. 26-31
    • Chaires, J.B.1
  • 98
    • 4143080522 scopus 로고    scopus 로고
    • Energetics of drug-DNA interactions
    • Chaires JB. Energetics of drug-DNA interactions. Biopolymers 1997;44:201-215
    • (1997) Biopolymers , vol.44 , pp. 201-215
    • Chaires, J.B.1
  • 99
    • 0031571628 scopus 로고    scopus 로고
    • Specific binding of Hoechst 33258 to the d(CGCAAATTTGCG)(2) duplex:calorimetric and spectroscopic studies
    • Haq I, Ladbury JE, Chowdhry BZ, Jenkins TC, Chaires JB. Specific binding of Hoechst 33258 to the d(CGCAAATTTGCG)(2) duplex:calorimetric and spectroscopic studies. J Mol Biol 1997;271:244-257
    • (1997) J Mol Biol , vol.271 , pp. 244-257
    • Haq, I.1    Ladbury, J.E.2    Chowdhry, B.Z.3    Jenkins, T.C.4    Chaires, J.B.5
  • 100
    • 48049103894 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies of Hoechst 33258:self-association and binding to non-cognate DNA
    • Buurma NJ, Haq I. Calorimetric and spectroscopic studies of Hoechst 33258:self-association and binding to non-cognate DNA. J Mol Biol 2008;381:607-621
    • (2008) J Mol Biol , vol.381 , pp. 607-621
    • Buurma, N.J.1    Haq, I.2
  • 101
    • 7744246534 scopus 로고    scopus 로고
    • Deciphering the origins of observed heat capacity changes for aminoglycoside binding to prokaryotic and eukaryotic ribosomal RNAa-sites:a calorimetric, computational, and osmotic stress study
    • Barbieri CM, Srinivasan AR, Pilch DS. Deciphering the origins of observed heat capacity changes for aminoglycoside binding to prokaryotic and eukaryotic ribosomal RNAa-sites:a calorimetric, computational, and osmotic stress study. J Am Chem Soc 2004;126:14380-14388
    • (2004) J Am Chem Soc , vol.126 , pp. 14380-14388
    • Barbieri, C.M.1    Srinivasan, A.R.2    Pilch, D.S.3
  • 102
    • 47649119769 scopus 로고    scopus 로고
    • Targeting DNA quadruplexes with distamycin a and its derivatives:an ITC and NMR study
    • Pagano B, Virno A, Mattia CA, Mayol L, Randazzo A, Giancola C. Targeting DNA quadruplexes with distamycin a and its derivatives:an ITC and NMR study. Biochimie 2008;90:1224-1232
    • (2008) Biochimie , vol.90 , pp. 1224-1232
    • Pagano, B.1    Virno, A.2    Mattia, C.A.3    Mayol, L.4    Randazzo, A.5    Giancola, C.6
  • 103
    • 57149104107 scopus 로고    scopus 로고
    • DNA-binding cytotoxic alkaloids:comparative study of the energetics of binding of berberine, palmatine, and coralyne
    • Bhadra K, Maiti M, Kumar GS. DNA-binding cytotoxic alkaloids:comparative study of the energetics of binding of berberine, palmatine, and coralyne. DNA Cell Biol 2008;27:675-685
    • (2008) DNA Cell Biol , vol.27 , pp. 675-685
    • Bhadra, K.1    Maiti, M.2    Kumar, G.S.3
  • 104
    • 84871139928 scopus 로고    scopus 로고
    • Isoquinoline alkaloids and their binding with DNA:calorimetry and thermal analysis applications
    • Bhadra K, Kumar GS. Isoquinoline alkaloids and their binding with DNA:calorimetry and thermal analysis applications. Mini-Rev Med Chem 2010;10:1235-1247
    • (2010) Mini-Rev Med Chem , vol.10 , pp. 1235-1247
    • Bhadra, K.1    Kumar, G.S.2
  • 105
    • 74149084926 scopus 로고    scopus 로고
    • Microcalorimetric and spectrographic studies on the interaction of DNA with betaxolol
    • Sun DZ, Xu XY, Liu M, Sun XJ, Zhang JY, Li LW, Di YY. Microcalorimetric and spectrographic studies on the interaction of DNA with betaxolol. Int J Pharm 2010;386:165-171
    • (2010) Int J Pharm , vol.386 , pp. 165-171
    • Sun, D.Z.1    Xu, X.Y.2    Liu, M.3    Sun, X.J.4    Zhang, J.Y.5    Li, L.W.6    Di, Y.Y.7
  • 106
    • 58549090881 scopus 로고    scopus 로고
    • Spectroscopic and calorimetric studies on the DNA recognition of pyrrolo 2,1-c 1,4 benzodiazepine hybrids
    • Rettig M, Kamal A, Ramu R, Mikolajczak J, Weisz K. Spectroscopic and calorimetric studies on the DNA recognition of pyrrolo 2,1-c 1,4 benzodiazepine hybrids. Bioorg Med Chem 2009;17:919-928
    • (2009) Bioorg Med Chem , vol.17 , pp. 919-928
    • Rettig, M.1    Kamal, A.2    Ramu, R.3    Mikolajczak, J.4    Weisz, K.5
  • 107
    • 35348960392 scopus 로고    scopus 로고
    • Daunomycin binding to detergent micelles:a model system for evaluating the hydrophobic contribution to drug-DNA interactions
    • Dignam JD, Qu XG, Ren JS, Chaires JB. Daunomycin binding to detergent micelles:a model system for evaluating the hydrophobic contribution to drug-DNA interactions. J Phys Chem B 2007;111:11576-11584
    • (2007) J Phys Chem B , vol.111 , pp. 11576-11584
    • Dignam, J.D.1    Qu, X.G.2    Ren, J.S.3    Chaires, J.B.4
  • 108
    • 0142040363 scopus 로고    scopus 로고
    • Enthalpy/entropy compensation:influence of DNA flanking sequence on the binding of 7-amino actinomycin → to its primary binding site in short DNA duplexes
    • Qu XG, Ren JS, Riccelli PV, Benight AS, Chaires JB. Enthalpy/entropy compensation:influence of DNA flanking sequence on the binding of 7-amino actinomycin → to its primary binding site in short DNA duplexes. Biochemistry 2003;42:11960-11967
    • (2003) Biochemistry , vol.42 , pp. 11960-11967
    • Qu, X.G.1    Ren, J.S.2    Riccelli, P.V.3    Benight, A.S.4    Chaires, J.B.5
  • 109
    • 0034713855 scopus 로고    scopus 로고
    • Energetics of DNA intercalation reactions
    • Ren JS, Jenkins TC, Chaires JB. Energetics of DNA intercalation reactions. Biochemistry 2000;39:8439-8447
    • (2000) Biochemistry , vol.39 , pp. 8439-8447
    • Ren, J.S.1    Jenkins, T.C.2    Chaires, J.B.3
  • 110
    • 0034581523 scopus 로고    scopus 로고
    • Parsing free energies of drug-DNA interactions
    • In:Michael L, Johnson GKA, editors, San Diego, CA:Academic Press
    • Haq I, Jenkins TC, Chowdhry BZ, Ren J, Chaires JB. Parsing free energies of drug-DNA interactions. In:Michael L, Johnson GKA, editors. Methods in Enzymology. San Diego, CA:Academic Press; 2000. p 373-405.
    • (2000) Methods in Enzymology , pp. 373-405
    • Haq, I.1    Jenkins, T.C.2    Chowdhry, B.Z.3    Ren, J.4    Chaires, J.B.5
  • 111
    • 0033815251 scopus 로고    scopus 로고
    • Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor
    • Velazquez-Campoy A, Luque I, Todd MJ, Milutinovich M, Kiso Y, Freire E. Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor. Protein Sci 2000;9:1801-1809
    • (2000) Protein Sci , vol.9 , pp. 1801-1809
    • Velazquez-Campoy, A.1    Luque, I.2    Todd, M.J.3    Milutinovich, M.4    Kiso, Y.5    Freire, E.6
  • 112
    • 78649300643 scopus 로고    scopus 로고
    • Pharmacophore model for pentamidine analogs active against Plasmodium falciparum
    • Athri P, Wenzler T, Tidwell R, Bakunova SM, Wilson WD. Pharmacophore model for pentamidine analogs active against Plasmodium falciparum. Eur J Med Chem 2010;45:6147-6151
    • (2010) Eur J Med Chem , vol.45 , pp. 6147-6151
    • Athri, P.1    Wenzler, T.2    Tidwell, R.3    Bakunova, S.M.4    Wilson, W.D.5
  • 114
    • 33846527387 scopus 로고    scopus 로고
    • Survey of the year 2005:literature on applications of isothermal titration calorimetry
    • Ababou A, Ladbury JE. 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
  • 115
    • 52649127984 scopus 로고    scopus 로고
    • A survey of the year 2007:literature on applications of isothermal titration calorimetry
    • Bjelic S, Jelesarov I. A survey of the year 2007:literature on applications of isothermal titration calorimetry. J Mol Recognit 2008;21:289-311
    • (2008) J Mol Recognit , vol.21 , pp. 289-311
    • Bjelic, S.1    Jelesarov, I.2
  • 116
    • 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
  • 117
    • 0842310293 scopus 로고    scopus 로고
    • A survey of the year 2002:literature on applications of isothermal titration calorimetry
    • Cliff MJ, Ladbury JE. A survey of the year 2002:literature on applications of isothermal titration calorimetry. J Mol Recognit 2003;16:383-391
    • (2003) J Mol Recognit , vol.16 , pp. 383-391
    • Cliff, M.J.1    Ladbury, J.E.2
  • 118
    • 39749105201 scopus 로고    scopus 로고
    • A survey of the year 2006:literature on applications of isothermal titration calorimetry
    • Okhrimenko O, Jelesarov M. 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
    • Okhrimenko, O.1    Jelesarov, M.2
  • 119
    • 0036169718 scopus 로고    scopus 로고
    • The binding database:data management and interface design
    • Chen X, Lin YM, Liu M, Gilson MK. The binding database:data management and interface design. Bioinformatics 2002;18:130-139
    • (2002) Bioinformatics , vol.18 , pp. 130-139
    • Chen, X.1    Lin, Y.M.2    Liu, M.3    Gilson, M.K.4
  • 120
    • 43949128085 scopus 로고    scopus 로고
    • PDBcal:a comprehensive dataset for receptor-ligand interactions with three-dimensional structures and binding thermodynamics from isothermal titration calorimetry
    • Li LW, Dantzer JJ, Nowacki J, O'Callaghan BJ, Meroueh SO. PDBcal:a comprehensive dataset for receptor-ligand interactions with three-dimensional structures and binding thermodynamics from isothermal titration calorimetry. Chem Biol Drug Des 2008;71:529-532
    • (2008) Chem Biol Drug Des , vol.71 , pp. 529-532
    • Li, L.W.1    Dantzer, J.J.2    Nowacki, J.3    O'Callaghan, B.J.4    Meroueh, S.O.5
  • 121
    • 79959972140 scopus 로고    scopus 로고
    • Investigating a macromolecular complex:the toolkit of methods
    • Perrakis A, Musacchio A, Cusack S, Petosa C. Investigating a macromolecular complex:the toolkit of methods. J Struct Biol 2011;175:106-112
    • (2011) J Struct Biol , vol.175 , pp. 106-112
    • Perrakis, A.1    Musacchio, A.2    Cusack, S.3    Petosa, C.4
  • 122
    • 77955841076 scopus 로고    scopus 로고
    • An easy-to-use tool for planning and modeling a calorimetric titration
    • Biswas T, Tsodikov OV. An easy-to-use tool for planning and modeling a calorimetric titration. Anal Biochem 2010;406:91-93
    • (2010) Anal Biochem , vol.406 , pp. 91-93
    • Biswas, T.1    Tsodikov, O.V.2
  • 123
    • 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 JCD, Brown PH, Bowden B,Yamaguchi H, Appella E, Samelson LE, Schuck P. 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 2007;16:30-42
    • (2007) Protein Sci , vol.16 , 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
  • 124
    • 83455169212 scopus 로고    scopus 로고
    • A critical approach to the thermodynamic characterization of inclusion complexes:multipletemperature isothermal titration calorimetric studies of native cyclodextrins with sodium dodecyl sulfate
    • Brocos P, Banquy X, Díaz-Vergara N, Pérez-Casas S, Pinẽiro Á , Costas M. A critical approach to the thermodynamic characterization of inclusion complexes:multipletemperature isothermal titration calorimetric studies of native cyclodextrins with sodium dodecyl sulfate. J Phys Chem B 2011;115:14381-14396
    • (2011) J Phys Chem B , vol.115 , pp. 14381-14396
    • Brocos, P.1    Banquy, X.2    Díaz-Vergara, N.3    Pérez-Casas, S.4    Pinẽiro Á5    Costas, M.6
  • 125
    • 78651153505 scopus 로고
    • Study of heat denaturation of DNA by use of the adiabatic microcalorimeter
    • Privalov PL, Kafiani KA, Monaselidze DR. Study of heat denaturation of DNA by use of the adiabatic microcalorimeter. Dokl Akad Nauk SSSR 1964;156:951-953
    • (1964) Dokl Akad Nauk SSSR , vol.156 , pp. 951-953
    • Privalov, P.L.1    Kafiani, K.A.2    Monaselidze, D.R.3
  • 127
    • 49949145384 scopus 로고
    • Hydration of macromolecules in native and denatured states
    • Privalov PL, Mrevlishvili GM. Hydration of macromolecules in native and denatured states. Biofizika 1967;12:22-29
    • (1967) Biofizika , vol.12 , pp. 22-29
    • Privalov, P.L.1    Mrevlishvili, G.M.2
  • 129
    • 78649674883 scopus 로고    scopus 로고
    • Protein heat capacity:an anomaly that maybe never was
    • Cooper A. Protein heat capacity:an anomaly that maybe never was. J Phys Chem Lett 2010;1:3298-3304
    • (2010) J Phys Chem Lett , vol.1 , pp. 3298-3304
    • Cooper, A.1
  • 130
    • 62649101310 scopus 로고    scopus 로고
    • Microcalorimetry of proteins and their complexes
    • Privalov PL. Microcalorimetry of proteins and their complexes. Methods Mol Biol 2009;490:1-39
    • (2009) Methods Mol Biol , vol.490 , pp. 1-39
    • Privalov, P.L.1
  • 131
    • 27344436962 scopus 로고    scopus 로고
    • Measurements of binding thermodynamics in drug discovery
    • Holdgate GA, Ward WHJ. Measurements of binding thermodynamics in drug discovery. Drug Discov Today 2005;10:1543-1550
    • (2005) Drug Discov Today , vol.10 , pp. 1543-1550
    • Holdgate, G.A.1    Ward, W.H.J.2
  • 132
    • 77951977004 scopus 로고    scopus 로고
    • Protein kinetic stability
    • Sanchez-Ruiz JM. Protein kinetic stability. Biophys Chem 2010;148:1-15
    • (2010) Biophys Chem , vol.148 , pp. 1-15
    • Sanchez-Ruiz, J.M.1
  • 133
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelesarov I, Bosshard HR. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J Mol Recognit 1999;12:3-18
    • (1999) J Mol Recognit , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 134
    • 0028845120 scopus 로고
    • Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution
    • Privalov G, Kavina V, Freire E, Privalov PL. Precise scanning calorimeter for studying thermal properties of biological macromolecules in dilute solution. Anal Biochem 1995;232:79-85
    • (1995) Anal Biochem , vol.232 , pp. 79-85
    • Privalov, G.1    Kavina, V.2    Freire, E.3    Privalov, P.L.4
  • 136
    • 0031567782 scopus 로고    scopus 로고
    • The entropy cost of protein association
    • Tamura A, Privalov PL. The entropy cost of protein association. J Mol Biol 1997;273:1048-1060
    • (1997) J Mol Biol , vol.273 , pp. 1048-1060
    • Tamura, A.1    Privalov, P.L.2
  • 137
    • 0022555893 scopus 로고
    • Scanning microcalorimetry in studying temperature-induced changes in proteins
    • Privalov PL, Potekhin SA. Scanning microcalorimetry in studying temperature-induced changes in proteins. Methods Enzymol 1986;131:4-51
    • (1986) Methods Enzymol , vol.131 , pp. 4-51
    • Privalov, P.L.1    Potekhin, S.A.2
  • 138
    • 0029100232 scopus 로고
    • Extracting thermodynamic data from equilibrium melting curves for oligonucleotide order-disorder transitions
    • Breslauer KJ. Extracting thermodynamic data from equilibrium melting curves for oligonucleotide order-disorder transitions. Methods Enzymol 1995;259:221.
    • (1995) Methods Enzymol , vol.259 , pp. 221
    • Breslauer, K.J.1
  • 139
    • 34547868080 scopus 로고    scopus 로고
    • Thermodynamic problems in structural molecular biology
    • Privalov PL. Thermodynamic problems in structural molecular biology. Pure Appl Chem 2007;79:1445-1462
    • (2007) Pure Appl Chem , vol.79 , pp. 1445-1462
    • Privalov, P.L.1
  • 140
    • 0034581192 scopus 로고    scopus 로고
    • Problems and prospects in microcalorimetry of biological macromolecules
    • Privalov GP, Privalov PL. Problems and prospects in microcalorimetry of biological macromolecules. Energet Biol Macromol 2000;323(Pt C):31-62.
    • (2000) Energet Biol Macromol , vol.323 , Issue.PT C , pp. 31-62
    • Privalov, G.P.1    Privalov, P.L.2
  • 141
    • 33748265526 scopus 로고    scopus 로고
    • Stability of DNA duplexes containing GG, CC, AA, and TT mismatches
    • Tikhomirova A, Beletskaya IV, Chalikian TV. Stability of DNA duplexes containing GG, CC, AA, and TT mismatches. Biochemistry 2006;45:10563-10571
    • (2006) Biochemistry , vol.45 , pp. 10563-10571
    • Tikhomirova, A.1    Beletskaya, I.V.2    Chalikian, T.V.3
  • 143
    • 0018588511 scopus 로고
    • Stability of proteins:small globular proteins
    • Privalov PL. Stability of proteins:small globular proteins. Adv Protein Chem 1979;33:167-241
    • (1979) Adv Protein Chem , vol.33 , pp. 167-241
    • Privalov, P.L.1
  • 144
    • 0032512877 scopus 로고    scopus 로고
    • Linkage of protonation and anion binding to the folding of Sac7d
    • McCrary BS, Bedell J, Edmondson SP, Shriver JW. Linkage of protonation and anion binding to the folding of Sac7d. J Mol Biol 1998;276:203-224
    • (1998) J Mol Biol , vol.276 , pp. 203-224
    • McCrary, B.S.1    Bedell, J.2    Edmondson, S.P.3    Shriver, J.W.4
  • 145
    • 77954327253 scopus 로고    scopus 로고
    • The thermodynamics of protein folding:a critique of widely used quasi-thermodynamic interpretations and a restatement based on the Gibbs-Duhem relation and consistent with the phase rule
    • Pethica BA. The thermodynamics of protein folding:a critique of widely used quasi-thermodynamic interpretations and a restatement based on the Gibbs-Duhem relation and consistent with the phase rule. Phys Chem Chem Phys 2010;12:7445-7456
    • (2010) Phys Chem Chem Phys , vol.12 , pp. 7445-7456
    • Pethica, B.A.1
  • 146
    • 0026734102 scopus 로고
    • 2-Dimensional differential scanning calorimetry -simultaneous resolution of intrinsic protein structural energetics and ligand-binding interactions by global linkage analysis
    • Straume M, Freire E. 2-Dimensional differential scanning calorimetry -simultaneous resolution of intrinsic protein structural energetics and ligand-binding interactions by global linkage analysis. Anal Biochem 1992;203:259-268
    • (1992) Anal Biochem , vol.203 , pp. 259-268
    • Straume, M.1    Freire, E.2
  • 147
    • 0026719686 scopus 로고
    • Global analysis of biochemical and biophysical data
    • Beechem JM. Global analysis of biochemical and biophysical data. Methods Enzymol 1992;210:37-54
    • (1992) Methods Enzymol , vol.210 , pp. 37-54
    • Beechem, J.M.1
  • 149
    • 0025125438 scopus 로고
    • Cold denaturation of proteins
    • Privalov PL. Cold denaturation of proteins. Crit Rev Biochem Mol 1990;25:281-305
    • (1990) Crit Rev Biochem Mol , vol.25 , pp. 281-305
    • Privalov, P.L.1
  • 150
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure:a calorimetric study
    • Privalov P, Khechinashvili N. A thermodynamic approach to the problem of stabilization of globular protein structure:a calorimetric study. J Mol Biol 1974;86:665-684
    • (1974) J Mol Biol , vol.86 , pp. 665-684
    • Privalov, P.1    Khechinashvili, N.2
  • 151
    • 75649100485 scopus 로고    scopus 로고
    • Energetic signatures of single base bulges:thermodynamic consequences and biological implications
    • Minetti CASA, Remeta DP, Dickstein R, Breslauer KJ. Energetic signatures of single base bulges:thermodynamic consequences and biological implications. Nucleic Acids Res 2010;38:97-116
    • (2010) Nucleic Acids Res , vol.38 , pp. 97-116
    • Minetti, C.A.S.A.1    Remeta, D.P.2    Dickstein, R.3    Breslauer, K.J.4
  • 152
    • 77949885720 scopus 로고    scopus 로고
    • Impact of alpha-hydroxy-propanodeoxyguanine adducts on DNA duplex energetics:opposite base modulation and implications for mutagenicity and genotoxicity
    • Minetti CASA, Remeta DP, Johnson F, Iden CR, Breslauer KJ. Impact of alpha-hydroxy-propanodeoxyguanine adducts on DNA duplex energetics:opposite base modulation and implications for mutagenicity and genotoxicity. Biopolymers 2010;93:370-382
    • (2010) Biopolymers , vol.93 , pp. 370-382
    • Minetti, C.A.S.A.1    Remeta, D.P.2    Johnson, F.3    Iden, C.R.4    Breslauer, K.J.5
  • 153
    • 0028783875 scopus 로고
    • Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex
    • Plum GE, Grollman AP, Johnson F, Breslauer KJ. Influence of the oxidatively damaged adduct 8-oxodeoxyguanosine on the conformation, energetics, and thermodynamic stability of a DNA duplex. Biochemistry 1995;34:16148-16160
    • (1995) Biochemistry , vol.34 , pp. 16148-16160
    • Plum, G.E.1    Grollman, A.P.2    Johnson, F.3    Breslauer, K.J.4
  • 154
    • 0032902402 scopus 로고    scopus 로고
    • The calorimetric criterion for a two-state process revisited
    • Zhou YQ, Hall CK, Karplus M. The calorimetric criterion for a two-state process revisited. Protein Sci 1999;8:1064-1074
    • (1999) Protein Sci , vol.8 , pp. 1064-1074
    • Zhou, Y.Q.1    Hall, C.K.2    Karplus, M.3
  • 155
    • 0026567099 scopus 로고
    • The molecular-basis of cooperativity in protein folding -thermodynamic dissection of interdomain interactions in phosphoglycerate kinase
    • Freire E, Murphy KP, Sanchez-Ruiz JM, Galisteo ML, Privalov PL. The molecular-basis of cooperativity in protein folding -thermodynamic dissection of interdomain interactions in phosphoglycerate kinase. Biochemistry 1992;31:250-256
    • (1992) Biochemistry , vol.31 , pp. 250-256
    • Freire, E.1    Murphy, K.P.2    Sanchez-Ruiz, J.M.3    Galisteo, M.L.4    Privalov, P.L.5
  • 156
    • 0017098463 scopus 로고
    • Na+ effects on transitions of DNA and polynucleotides of variable linear charge density
    • Record MT, Woodbury CP, Lohman TM. Na+ effects on transitions of DNA and polynucleotides of variable linear charge density. Biopolymers 1976;15.
    • (1976) Biopolymers , pp. 15
    • Record, M.T.1    Woodbury, C.P.2    Lohman, T.M.3
  • 157
    • 0025999487 scopus 로고
    • Membrane binding induces lipid-specific changes in the denaturation profile of bovine prothrombin
    • Lentz B, Wu J, Sorrentino A, Carleton J. Membrane binding induces lipid-specific changes in the denaturation profile of bovine prothrombin. A scanning calorimetry study. Biophys J 1991;60:942-951
    • (1991) A scanning calorimetry study. Biophys J , vol.60 , pp. 942-951
    • Lentz, B.1    Wu, J.2    Sorrentino, A.3    Carleton, J.4
  • 158
    • 0000826487 scopus 로고
    • Biochemical applications of differential scanning calorimetry
    • Sturtevant JM. Biochemical applications of differential scanning calorimetry. Annu Rev Phys Chem 1987;38:463-488
    • (1987) Annu Rev Phys Chem , vol.38 , pp. 463-488
    • Sturtevant, J.M.1
  • 159
    • 0025005334 scopus 로고
    • Linked thermal and solute perturbation analysis of cooperative domain interactions in proteins
    • Ramsay G, Freire E. Linked thermal and solute perturbation analysis of cooperative domain interactions in proteins. Structural stability of diphtheria toxin. Biochemistry 1990;29:8677-8683
    • (1990) Structural stability of diphtheria toxin. Biochemistry , vol.29 , pp. 8677-8683
    • Ramsay, G.1    Freire, E.2
  • 161
    • 0035743381 scopus 로고    scopus 로고
    • Measurement and analysis of results obtained on biological substances with differential scanning calorimetry
    • Hinz HJ, Schwarz FP. Measurement and analysis of results obtained on biological substances with differential scanning calorimetry. Pure Appl Chem 2001;73:745-759
    • (2001) Pure Appl Chem , vol.73 , pp. 745-759
    • Hinz, H.J.1    Schwarz, F.P.2
  • 162
    • 0033053602 scopus 로고    scopus 로고
    • Energetics of solvent and ligandinduced conformational changes in alpha-lactalbumin
    • Griko YV, Remeta DP. Energetics of solvent and ligandinduced conformational changes in alpha-lactalbumin. Protein Sci 1999;8:554-561
    • (1999) Protein Sci , vol.8 , pp. 554-561
    • Griko, Y.V.1    Remeta, D.P.2
  • 163
    • 0033961193 scopus 로고    scopus 로고
    • A calorimetric study of the influence of calcium on the stability of bovine alphalactalbumin
    • Hendrix T, Griko YV, Privalov PL. A calorimetric study of the influence of calcium on the stability of bovine alphalactalbumin. Biophys Chem 2000;84:27-34
    • (2000) Biophys Chem , vol.84 , pp. 27-34
    • Hendrix, T.1    Griko, Y.V.2    Privalov, P.L.3
  • 164
    • 0037197677 scopus 로고    scopus 로고
    • Maximal stabilities of reversible two-state proteins
    • Kumar S, Tsai CJ, Nussinov R. Maximal stabilities of reversible two-state proteins. Biochemistry 2002;41:5359-5374
    • (2002) Biochemistry , vol.41 , pp. 5359-5374
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 165
    • 33747793145 scopus 로고    scopus 로고
    • Energetics of membrane protein folding and stability
    • Minetti CASA, Remeta DP. Energetics of membrane protein folding and stability. Arch Biochem Biophys 2006;453:32-53
    • (2006) Arch Biochem Biophys , vol.453 , pp. 32-53
    • Minetti, C.A.S.A.1    Remeta, D.P.2
  • 166
    • 0028038094 scopus 로고
    • Thermodynamic and structural stability of cytochrome-c-oxidase from Paracoccus denitrificans
    • Haltia T, Semo N, Arrondo JLR, Goni FM, Freire E. Thermodynamic and structural stability of cytochrome-c-oxidase from Paracoccus denitrificans. Biochemistry 1994;33:9731-9740
    • (1994) Biochemistry , vol.33 , pp. 9731-9740
    • Haltia, T.1    Semo, N.2    Arrondo, J.L.R.3    Goni, F.M.4    Freire, E.5
  • 167
    • 0032566609 scopus 로고    scopus 로고
    • Characterization of the structure, function, and conformational stability of PorB class 3 protein from Neisseria meningitidis
    • Minetti CASA, Blake MS, Remeta DP. Characterization of the structure, function, and conformational stability of PorB class 3 protein from Neisseria meningitidis. A porin with unusual physicochemical properties. J Biol Chem 1998;273:25329-25338
    • (1998) A porin with unusual physicochemical properties. J Biol Chem , vol.273 , pp. 25329-25338
    • Minetti, C.A.S.A.1    Blake, M.S.2    Remeta, D.P.3
  • 171
    • 4244028103 scopus 로고
    • Prediction of protein stability and folding unfolding thermodynamics from crystallographic structure
    • Murphy KP, Freire E. Prediction of protein stability and folding unfolding thermodynamics from crystallographic structure. FASEB J 1992;6:313-361
    • (1992) FASEB J , vol.6 , pp. 313-361
    • Murphy, K.P.1    Freire, E.2
  • 172
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry:the influenza hemagglutinin
    • Skehel JJ, Wiley DC. Receptor binding and membrane fusion in virus entry:the influenza hemagglutinin. Annu Rev Biochem 2000;69:531-569
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 173
    • 56949106817 scopus 로고    scopus 로고
    • Microcalorimetry:a response to challenges in modern biotechnology
    • Krell T. Microcalorimetry:a response to challenges in modern biotechnology. Microb Biotechnol 2008;1:126-136
    • (2008) Microb Biotechnol , vol.1 , pp. 126-136
    • Krell, T.1
  • 175
    • 0006456405 scopus 로고
    • Thermally induced unfolding of the tryptophan synthase alpha 2beta 2 multienzyme complex from Salmonella typhimurium
    • Remeta D, Miles E, Ginsburg A. Thermally induced unfolding of the tryptophan synthase alpha 2beta 2 multienzyme complex from Salmonella typhimurium. Pure Appl Chem 1995;67:1859-1866
    • (1995) Pure Appl Chem , vol.67 , pp. 1859-1866
    • Remeta, D.1    Miles, E.2    Ginsburg, A.3
  • 177
    • 0029968822 scopus 로고    scopus 로고
    • Improved nearestneighbor parameters for predictingDNAduplex stability
    • SantaLucia JJ, Allawi H, Seneviratne P. Improved nearestneighbor parameters for predictingDNAduplex stability. Biochemistry 1996;35:3555-3562
    • (1996) Biochemistry , vol.35 , pp. 3555-3562
    • SantaLucia, J.J.1    Allawi, H.2    Seneviratne, P.3
  • 178
    • 23144440350 scopus 로고    scopus 로고
    • DINAMelt web server for nucleic acid melting prediction
    • Markham NR, Zuker M. DINAMelt web server for nucleic acid melting prediction. Nucleic Acids Res. 2005;33:W577-W581.
    • (2005) Nucleic Acids Res. , vol.33
    • Markham, N.R.1    Zuker, M.2
  • 179
    • 0033529318 scopus 로고    scopus 로고
    • A more unified picture for the thermodynamics of nucleic acid duplex melting:a characterization by calorimetric and volumetric techniques
    • Chalikian TV, Volker J, Plum GE, Breslauer KJ. A more unified picture for the thermodynamics of nucleic acid duplex melting:a characterization by calorimetric and volumetric techniques, Proc Natl Acad Sci USA 1999;96:7853-7858.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 7853-7858
    • Chalikian, T.V.1    Volker, J.2    Plum, G.E.3    Breslauer, K.J.4
  • 180
    • 59949096896 scopus 로고    scopus 로고
    • DNA hydration studied by pressure perturbation scanning microcalorimetry
    • Dragan AI, Russell DJ, Privalov PL. DNA hydration studied by pressure perturbation scanning microcalorimetry. Biopolymers 2009;91:95-101
    • (2009) Biopolymers , vol.91 , pp. 95-101
    • Dragan, A.I.1    Russell, D.J.2    Privalov, P.L.3
  • 181
    • 0029933128 scopus 로고    scopus 로고
    • A highly salt-dependent enthalpy change for Escherichia coli SSB protein-nucleic acid binding due to ion-protein interactions
    • Lohman TM, Overman LB, Ferrari ME, Kozlov AG. A highly salt-dependent enthalpy change for Escherichia coli SSB protein-nucleic acid binding due to ion-protein interactions. Biochemistry 1996;35:5272-5279
    • (1996) Biochemistry , vol.35 , pp. 5272-5279
    • Lohman, T.M.1    Overman, L.B.2    Ferrari, M.E.3    Kozlov, A.G.4
  • 183
    • 0024281290 scopus 로고
    • Differential scanning colorimetry of the irreversible thermal denaturation of thermolysin
    • Sanchez-Ruiz JM, Lopez-Locomba JL, Cortijo M, Mateo PL. Differential scanning colorimetry of the irreversible thermal denaturation of thermolysin. Biochemistry 1988;27:1648-1652
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanchez-Ruiz, J.M.1    Lopez-Locomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 185
    • 0034237295 scopus 로고    scopus 로고
    • Lower kinetic limit to protein thermal stability:a proposal regarding protein stability in vivo and its relation with misfolding diseases
    • del Pino IMP, Ibarra-Molero B, Sanchez-Ruiz JM. Lower kinetic limit to protein thermal stability:a proposal regarding protein stability in vivo and its relation with misfolding diseases. Prot Struct Funct Genet 2000;40:58-70
    • (2000) Prot Struct Funct Genet , vol.40 , pp. 58-70
    • del Pino, I.M.P.1    Ibarra-Molero, B.2    Sanchez-Ruiz, J.M.3


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