LEADER 05279nam 22006494a 450 001 9910143744003321 005 20170815121636.0 010 $a1-280-27608-8 010 $a9786610276080 010 $a0-470-01112-2 010 $a0-470-01111-4 035 $a(CKB)1000000000356146 035 $a(EBL)239032 035 $a(OCoLC)475950107 035 $a(SSID)ssj0000111592 035 $a(PQKBManifestationID)11137687 035 $a(PQKBTitleCode)TC0000111592 035 $a(PQKBWorkID)10080743 035 $a(PQKB)10017079 035 $a(MiAaPQ)EBC239032 035 $a(EXLCZ)991000000000356146 100 $a20040412d2004 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aBiocalorimetry 2$b[electronic resource] $eapplications of calorimetry in the biological sciences /$fedited by John E. Ladbury, Michael L. Doyle 205 $a2nd ed. 210 $aChichester ;$aHoboken, NJ $cWiley$dc2004 215 $a1 online resource (277 p.) 300 $aRev. ed. of: Biocalorimetry. 311 $a0-470-84968-1 320 $aIncludes bibliographical references and index. 327 $aBiocalorimetry 2; Contents; Preface; List of Contributors; Part I General Introduction; 1 Applications of Biocalorimetry: Binding, Stability and Enzyme Kinetics; 1.1 Introduction; 1.2 Principles of isothermal titration calorimetry (ITC); 1.3 Applications of ITC in the life sciences; 1.4 Thermodynamic signatures of non-covalent interactions; 1.5 Thermodynamic discrimination (TD); 1.6 ITC as a tool for studying drug-DNA interactions; 1.7 ITC as a tool for studying protein-DNA interactions; 1.8 The application of calorimetry for examining hydration effcts 327 $a1.9 The use of ITC for studying the kinetics and thermodynamics of enzyme catalysis1.10 Principles of differential scanning calorimetry (DSC); 1.11 Applications of DSC in the life sciences; 1.12 Thermodynamic stability; 1.13 Shelf life versus thermodynamic stability; 1.14 Specific and non-specific binding; 1.15 Intrinsic and extrinsic macromolecular stability; 1.16 Oligomerization; 1.17 The use of DSC for examining nucleic acid helix coil transitions; 1.18 Summary; Acknowledgements; References; Part II Isothermal Titration Calorimetry; 2 Isothermal Titration Calorimetry: A Tutorial 327 $a2.1 Introduction2.2 Thermodynamic characterization; 2.3 Instrumentation; 2.4 Raw data; 2.5 Basic considerations for experimental set-up; 2.6 Data analysis; 2.7 Summary; Application notes; Acknowledgement; References; 3 The Application of Isothermal Titration Calorimetry to Drug Discovery; 3.1 Introduction; 3.2 Overview of the drug discovery process; 3.3 Experimental measurement of thermodynamic binding parameters; 3.4 ITC in drug discovery; 3.5 Summary; References; 4 Dissecting the Thermodynamics of DNA-Protein Interactions; 4.1 Introduction; 4.2 Model systems 327 $a4.3 Comparison with the hydrophobic effect4.4 Protonation and charged-charged hydrogen bonds; 4.5 Dissection of the binding entropy; 4.6 Entropy contributions to the Sso7d-DNA interaction; 4.7 Entropy contributions to the GCN4-DNA interaction; 4.8 Discussion; Acknowledgements; References; 5 Salt Effects in Ribonuclease-Ligand Interactions: Screening or Competitive Binding?; 5.1 Introduction; 5.2 Anion binding to a protein-protein complex; 5.3 Charge-charge interactions in ribonuclease binding; 5.4 Conclusions; Acknowledgement; References 327 $a6 Thermodynamics-Structure Correlations of Sulfonamide Inhibitor Binding to Carbonic Anhydrase6.1 Introduction; 6.2 Identification of protonation reactions occurring upon binding; 6.3 Observed thermodynamics of inhibitor binding to CA; 6.4 Energetics of inhibitor protonation; 6.5 Sulfonamide 'anion' binding thermodynamics; 6.6 Correlations between structures and the thermodynamics of sulfonamide binding to CA; 6.7 Conclusions; References; 7 Energetics of the Interaction of Human Acidic Fibroblast Growth Factor with Heparin and the Functional Analogue Myo-Inositol Hexasulfate; 7.1 Introduction 327 $a7.2 Thermodynamic parameter derived from ITC experiments 330 $aOver the last decade, high-sensitivity calorimetry has developed from a specialist method used mainly by dedicated experts to a major, commercially available tool in the arsenal directed at understanding molecular interactions and stability. Calorimeters have now become commonplace in bioscience laboratories. As a result, the number of those proficient in experimentation in this field has risen dramatically, as has the range of experiments to which these methods have been applied. Applications extend from studies in small molecule and solvent biophysics, through drug screening to whole cell as 606 $aCalorimetry 606 $aBiology$xTechnique 608 $aElectronic books. 615 0$aCalorimetry. 615 0$aBiology$xTechnique. 676 $a572.43 676 $a572.436 701 $aLadbury$b John E.$f1960-$0880077 701 $aDoyle$b Michael L.$f1959-$0880078 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910143744003321 996 $aBiocalorimetry 2$91965145 997 $aUNINA