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Volumn 37, Issue 6, 2004, Pages 885-887

Application of isothermal titration calorimetry in the biological sciences: Things are heating up!

Author keywords

[No Author keywords available]

Indexed keywords

ACCURACY; BINDING AFFINITY; BIOMEDICINE; CALORIMETRY; CHEMICAL ANALYSIS; CHEMICAL BINDING; CHEMICAL BOND; CHEMICAL STRUCTURE; COMPLEX FORMATION; CONCENTRATION (PARAMETERS); CORRELATION ANALYSIS; CYTOLOGY; ELECTRICITY; ENERGY; ENTHALPY; ENTROPY; EXPERIMENT; HEAT; IMMOBILIZATION; INSTRUMENT; ISOTHERMAL TITRATION CALORIMETRY; LABORATORY; MEASUREMENT; MOLECULAR INTERACTION; MOLECULE; PARAMETER; PH; PROTON TRANSPORT; QUANTITATIVE ANALYSIS; REVIEW; SCREENING; SENSOR; STRUCTURE ANALYSIS; SUSPENSION; TEMPERATURE; THERMODYNAMICS; TITRIMETRY;

EID: 10044226082     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/04376te01     Document Type: Review
Times cited : (63)

References (19)
  • 1
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman, T., S. Williston, J.F. Brandts, and L.N. Lin. 1989. Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Anal. Biochem. 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
  • 2
  • 3
    • 0029645119 scopus 로고
    • Counting the calories to stay in the groove
    • Ladbury, J.E. 1995. Counting the calories to stay in the groove. Structure 3:635-639.
    • (1995) Structure , vol.3 , pp. 635-639
    • Ladbury, J.E.1
  • 4
    • 0030266484 scopus 로고    scopus 로고
    • Sensing the heat: The application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions
    • Ladbury, J.E. and B.Z. Chowdhry. 1996. Sensing the heat: the application of isothermal titration calorimetry to thermodynamic studies of biomolecular interactions. Chem. Biol. 3:791-801.
    • (1996) Chem. Biol. , vol.3 , pp. 791-801
    • Ladbury, J.E.1    Chowdhry, B.Z.2
  • 5
    • 0032901515 scopus 로고    scopus 로고
    • Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition
    • Jelasarov, I. and H.R. Bosshard. 1999. Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J. Mol. Recogn. 12:3-18.
    • (1999) J. Mol. Recogn. , vol.12 , pp. 3-18
    • Jelasarov, I.1    Bosshard, H.R.2
  • 6
    • 4744338722 scopus 로고    scopus 로고
    • The extended interface: Measuring non-local effects in biomolecular interactions
    • Williams, M.A. and J.E. Ladbury. 2004. The extended interface: measuring non-local effects in biomolecular interactions. Curr. Opin Struct. Biol. 14:562-569.
    • (2004) Curr. Opin Struct. Biol. , vol.14 , pp. 562-569
    • Williams, M.A.1    Ladbury, J.E.2
  • 9
    • 0032574705 scopus 로고    scopus 로고
    • Molecular basis of resistance to HIV-1 protease inhibition: A plausible hypothesis
    • Luque, I., M.J. Todd, J. Gomez, N. Semo, and E. Freire. 1998. Molecular basis of resistance to HIV-1 protease inhibition: a plausible hypothesis. Biochemistry 37:5791-5797.
    • (1998) Biochemistry , vol.37 , pp. 5791-5797
    • Luque, I.1    Todd, M.J.2    Gomez, J.3    Semo, N.4    Freire, E.5
  • 10
    • 0029832524 scopus 로고    scopus 로고
    • Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry
    • Baker, B.M. and K.P. Murphy. 1996. Evaluation of linked protonation effects in protein binding reactions using isothermal titration calorimetry. Biophys. J. 71:2049-2055.
    • (1996) Biophys. J. , vol.71 , pp. 2049-2055
    • Baker, B.M.1    Murphy, K.P.2
  • 11
    • 0034713855 scopus 로고    scopus 로고
    • Energetics of DNA intercalation reactions
    • Ren, J.S., T.C. Jenkins, and J.B. Chaires. 2000. Energetics of DNA intercalation reactions. Biochemistry 39:8439-8447.
    • (2000) Biochemistry , vol.39 , pp. 8439-8447
    • Ren, J.S.1    Jenkins, T.C.2    Chaires, J.B.3
  • 12
    • 0035846564 scopus 로고    scopus 로고
    • Specific DNA recognition by the type II restriction endonuclease MunI: The effect of pH
    • Haq, I., R. O'Brien, A. Lagunavicius, V. Siksnys, and J. Ladbury. 2001. Specific DNA recognition by the type II restriction endonuclease MunI: the effect of pH. Biochemistry 40:14960-14967.
    • (2001) Biochemistry , vol.40 , pp. 14960-14967
    • Haq, I.1    O'Brien, R.2    Lagunavicius, A.3    Siksnys, V.4    Ladbury, J.5
  • 13
    • 1042298819 scopus 로고    scopus 로고
    • Heat capacity effects of water molecules and ions at a protein-DNA interface
    • Bergqvist, S., M.A. Williams, R. O'Brien, and J.E. Ladbury. 2004. Heat capacity effects of water molecules and ions at a protein-DNA interface. J. Mol. Biol. 336:829-842.
    • (2004) J. Mol. Biol. , vol.336 , pp. 829-842
    • Bergqvist, S.1    Williams, M.A.2    O'Brien, R.3    Ladbury, J.E.4
  • 14
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R.S. and M.T. Record, Jr. 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science 263:777-783.
    • (1994) Science , vol.263 , pp. 777-783
    • Spolar, R.S.1    Record Jr., M.T.2
  • 15
    • 0029080864 scopus 로고
    • Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin
    • Gomez, J. and E. Freire. 1995 Thermodynamic mapping of the inhibitor site of the aspartic protease endothiapepsin. J. Mol. Biol. 252:337-350.
    • (1995) J. Mol. Biol. , vol.252 , pp. 337-350
    • Gomez, J.1    Freire, E.2
  • 16
    • 0029860343 scopus 로고    scopus 로고
    • Water mediated protein-DNA interactions: The relationship of thermodynamics to structural detail
    • Morton, C.J. and J.E. Ladbury. 1996. Water mediated protein-DNA interactions: the relationship of thermodynamics to structural detail. Prot. Sci. 5:2115-2118.
    • (1996) Prot. Sci. , vol.5 , pp. 2115-2118
    • Morton, C.J.1    Ladbury, J.E.2
  • 17
    • 0033778163 scopus 로고    scopus 로고
    • Comparison of binding energies of SrcSH2-phosphotyrosyl peptides with structure-based prediction using surface area based empirical parameterization
    • Henriques, D.A., J.E. Ladbury, and R.M. Jackson. 2000. Comparison of binding energies of SrcSH2-phosphotyrosyl peptides with structure-based prediction using surface area based empirical parameterization. Prot. Sci. 9:1975-1985.
    • (2000) Prot. Sci. , vol.9 , pp. 1975-1985
    • Henriques, D.A.1    Ladbury, J.E.2    Jackson, R.M.3
  • 18
    • 0027991944 scopus 로고
    • Thermodynamic and structural consequences of changing a sulphur atom to a methylene group in the M13Nle mutation in ribonuclease S
    • Thomson, J., G.S. Ratnaparkhi, R. Varadarajan, J.M. Sturtevant, and F.M. Richards. 1994. Thermodynamic and structural consequences of changing a sulphur atom to a methylene group in the M13Nle mutation in ribonuclease S. Biochemistry 33:8587-8593.
    • (1994) Biochemistry , vol.33 , pp. 8587-8593
    • Thomson, J.1    Ratnaparkhi, G.S.2    Varadarajan, R.3    Sturtevant, J.M.4    Richards, F.M.5
  • 19
    • 27244462484 scopus 로고    scopus 로고
    • Inhibitors to the Src SH2 domain: A lesson in thermodynamic structural correlation in drug design
    • Henriques, D.A. and J.E. Ladbury. 2001. Inhibitors to the Src SH2 domain: a lesson in thermodynamic structural correlation in drug design. Arch. Biochem. Biophys. 390:158-168.
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 158-168
    • Henriques, D.A.1    Ladbury, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.