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Isothermal titration calorimetry.
| Content Provider | Semantic Scholar |
|---|---|
| Copyright Year | 2005 |
| Abstract | Isothermal titration calorimetry is an ideal technique for measuring biological binding interactions. It does not rely on the presence of chromophores or fluorophores, nor does it require an enzymatic assay. Because the technique relies only on the detection of a heat effect upon binding, it can be used to measure the binding constant, K, the enthalpy of binding, DeltaH degrees and the stoichiometry, or number of binding sites, n. This chapter describes instrumentation, experimental design, and the theoretical underpinnings necessary to run and analyze a calorimetric binding experiment. |
| Starting Page | 1 |
| Ending Page | 16 |
| Page Count | 16 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | https://static-content.springer.com/esm/art:10.1186%2F1471-2105-13-79/MediaObjects/12859_2011_5278_MOESM7_ESM.pdf |
| Alternate Webpage(s) | http://www.iiserpune.ac.in/~cathale/lects/2011monsoon/bio322-student/019.pdf |
| PubMed reference number | 15939991v1 |
| Volume Number | 305 |
| Journal | Methods in molecular biology |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Binding Sites Calorimetry Enzyme Assays Titration Method |
| Content Type | Text |
| Resource Type | Article |
