LEADER 05373nam 22006974a 450 001 9911019250203321 005 20200520144314.0 010 $a9786610276080 010 $a9781280276088 010 $a1280276088 010 $a9780470011126 010 $a0470011122 010 $a9780470011119 010 $a0470011114 035 $a(CKB)1000000000356146 035 $a(EBL)239032 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(OCoLC)85820369 035 $a(Perlego)2752792 035 $a(EXLCZ)991000000000356146 100 $a20040412d2004 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aBiocalorimetry 2 $eapplications of calorimetry in the biological sciences /$fedited by John E. Ladbury, Michael L. Doyle 205 $a2nd ed. 210 $aChichester ;$aHoboken, NJ $cWiley$dc2004 215 $a1 online resource (277 p.) 300 $aRev. ed. of: Biocalorimetry. 311 08$a9780470849682 311 08$a0470849681 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 517 3 $aBiocalorimetry two 606 $aCalorimetry 606 $aBiology$xTechnique 615 0$aCalorimetry. 615 0$aBiology$xTechnique. 676 $a572/.43 701 $aLadbury$b John E.$f1960-$01841394 701 $aDoyle$b Michael L.$f1959-$01841395 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9911019250203321 996 $aBiocalorimetry 2$94421118 997 $aUNINA LEADER 01119nas# 22002651i 450 001 UON00236667 005 20231205103528.660 011 $a0030-9729 100 $a20030730f1968 |0itac50 ba 101 $aeng 102 $aUN 105 $a|||| 1|||| 110 $aaQ||||||||| 200 1 $aˆThe ‰Pakistan Development Review$eThe Quarterly Journal of the Pakistan Institu te of Development Ecomics$fPakistan Institute of Development Economics 210 $aKara chi$cPakistan Institute of Development Economic 300 $aTrimestrale 316 $a59*$5IT-UONSI RIV B173 606 $aEconomia$xPeriodici$3UONC035861$2FI 712 02$aPakistan Institute of Development Economics$3UONV102261 801 $aIT$bSOL$c20250919$gRICA 899 $aSIBA - SISTEMA BIBLIOTECARIO DI ATENEO$2UONSI$48(1968) » 9(1969)*C*$cRIV B 173 ; 912 $aUON00236667 950 $aSIBA - SISTEMA BIBLIOTECARIO DI ATENEO$bSI 8(1968) » 9(1969)*C*$dSI 173 $eSI SC 59 5 59* 996 $aPakistan development review$9976814 997 $aUNIOR