- Abstract:
-
The high-throughput characterization of solution binding equilibria is essential in biomedical research such as drug design as well as in material applications of synthetic systems in which reversible binding interactions play critical roles. Although isothermal titration calorimetry (ITC) has been widely employed for describing such binding events, factors such as speed, concentration, and sample complexity would principally favor a mass spectrometry approach. Here, we show a link between IT...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/jp102933h
-
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- Journal:
- The journal of physical chemistry. B
- Volume:
- 114
- Issue:
- 26
- Pages:
- 8606-8615
- Publication date:
- 2010-07-05
- DOI:
- EISSN:
-
1520-5207
- ISSN:
-
1520-6106
- URN:
-
uuid:63e1392e-aadf-4fb9-8350-c077b3027467
- Source identifiers:
-
60302
- Local pid:
- pubs:60302
- Copyright date:
- 2010
Journal article
Correlating solution binding and ESI-MS stabilities by incorporating solvation effects in a confined cucurbit[8]uril system.
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