메뉴 건너뛰기




Volumn 1008, Issue , 2013, Pages 103-118

Isothermal titration calorimetry for studying protein-ligand interactions

Author keywords

Affinity constant; Binding constant; Competition experiments; Dissociation constant; Drug discovery; Enthalpy change; Entropy change; Equilibrium constant; Gibbs free energy change; Heat capacity change; Hydrogen bond; Hydrophobic interactions; Isothermal titration calorimetry; ITC; Lead discovery; Lead optimization; Ligand binding; Protein interactions; Stoichiometry; Thermodynamics

Indexed keywords

LIGAND; PROTEIN; PROTEIN BINDING;

EID: 84925559402     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-398-5_4     Document Type: Article
Times cited : (64)

References (17)
  • 1
    • 74149083849 scopus 로고    scopus 로고
    • Adding calorimetric data to decision making in lead discovery: A hot tip
    • Ladbury JE, Klebe G, Freire E (2010) Adding calorimetric data to decision making in lead discovery: A hot tip. Nat Rev Drug Discov 9:23-27
    • (2010) Nat Rev Drug Discov , vol.9 , pp. 23-27
    • Ladbury, J.E.1    Klebe, G.2    Freire, E.3
  • 3
    • 27344436962 scopus 로고    scopus 로고
    • Measurements of binding thermodynamics in drug discovery
    • Holdgate GA, Ward WHJ (2005) Measurements of binding thermodynamics in drug discovery. Drug Discov Today 10:1543-1550
    • (2005) Drug Discov Today , vol.10 , pp. 1543-1550
    • Holdgate, G.A.1    Ward, W.H.J.2
  • 4
    • 0024356301 scopus 로고
    • Rapid measurement of binding constants and heats of binding using a new titration calorimeter
    • Wiseman T et al (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
  • 5
    • 0035226253 scopus 로고    scopus 로고
    • Isothermal titration calorimetry in drug discovery
    • Ward WHJ, Holdgate GA (2001) Isothermal titration calorimetry in drug discovery. Prog Med Chem 38:309-376
    • (2001) Prog Med Chem , vol.38 , pp. 309-376
    • Ward, W.H.J.1    Holdgate, G.A.2
  • 6
    • 0002638463 scopus 로고
    • Heat capacity and entropy changes in processes involving proteins
    • Sturtevant JM (1977) Heat capacity and entropy changes in processes involving proteins. Proc Natl Acad Sci U S A 74:2236-2240
    • (1977) Proc Natl Acad Sci U S A , vol.74 , pp. 2236-2240
    • Sturtevant, J.M.1
  • 7
    • 0037044316 scopus 로고    scopus 로고
    • Positive heat capacity change upon specific binding of translation initiation factor eIF4E to mRNA 5cap
    • Niedzwiecka A et al (2002) Positive heat capacity change upon specific binding of translation initiation factor eIF4E to mRNA 5cap. Biochemistry 41:12140-12148
    • (2002) Biochemistry , vol.41 , pp. 12140-12148
    • Niedzwiecka, A.1
  • 9
    • 0031670461 scopus 로고    scopus 로고
    • Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride
    • Fukada H, Takahashi K (1998) Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride. Proteins 33:159-166
    • (1998) Proteins , vol.33 , pp. 159-166
    • Fukada, H.1    Takahashi, K.2
  • 10
    • 0035442411 scopus 로고    scopus 로고
    • Directmeasurement of protein binding energetics by isothermal titration calorimetry
    • Leavitt S, FreireE(2001)Directmeasurement of protein binding energetics by isothermal titration calorimetry. Curr Opin Struct Biol 11:560-566
    • (2001) Curr Opin Struct Biol , vol.11 , pp. 560-566
    • Leavitt, S.1    Freiree2
  • 11
    • 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 (1999) Isothermal titration calorimetry and differential scanning calorimetry as complementary tools to investigate the energetics of biomolecular recognition. J Mol Recognit 12:3-18
    • (1999) J Mol Recognit , vol.12 , pp. 3-18
    • Jelesarov, I.1    Bosshard, H.R.2
  • 13
    • 0035884687 scopus 로고    scopus 로고
    • Enzyme kinetics determined using calorimetry: A general assay for enzyme activity
    • Todd MJ, Gomez J (2001) Enzyme kinetics determined using calorimetry: A general assay for enzyme activity? Anal Biochem 296:179-187
    • (2001) Anal Biochem , vol.296 , pp. 179-187
    • Todd, M.J.1    Gomez, J.2
  • 14
    • 2942552633 scopus 로고    scopus 로고
    • The abrf-mirg02 study: Assembly state, thermodynamic and kinetic analysis of an enzyme/inhibitor interaction
    • Myszka DG et al (2003) The ABRF-MIRG02 study: Assembly state, thermodynamic and kinetic analysis of an enzyme/inhibitor interaction. J Biomol Tech 14:247-269
    • (2003) J Biomol Tech , vol.14 , pp. 247-269
    • Myszka, D.G.1
  • 15
    • 0032577337 scopus 로고    scopus 로고
    • The effects of salt on the TATA binding protein-DNA interaction from a hyperthermophilic archaeon
    • OBrien R et al (1998) The effects of salt on the TATA binding protein-DNA interaction from a hyperthermophilic archaeon. J Mol Biol 279:117-125
    • (1998) J Mol Biol , vol.279 , pp. 117-125
    • Obrien, R.1
  • 16
    • 0345293146 scopus 로고    scopus 로고
    • On the value of c can low affinity systems be studied by isothermal titration calorimetry
    • Turnbull WB, Daranas AH (2003) On the value of c: Can low affinity systems be studied by isothermal titration calorimetry? J Am Chem Soc 125:14859-14866
    • (2003) J Am Chem Soc , vol.125 , pp. 14859-14866
    • Turnbull, W.B.1    Daranas, A.H.2
  • 17
    • 34250641961 scopus 로고    scopus 로고
    • Isothermal titration calorimetry to determine association constants for high-Affinity ligands
    • Velazquez-Campoy A, Freire E (2006) Isothermal titration calorimetry to determine association constants for high-Affinity ligands. Nat Protoc 1:186-191
    • (2006) Nat Protoc , vol.1 , pp. 186-191
    • Velazquez-Campoy, A.1    Freire, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.