| Autor: |
Riggle BA; Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, USA. ivandmo@sas.upenn.edu., Greenberg ML, Wang Y, Wissner RF, Zemerov SD, Petersson EJ, Dmochowski IJ |
| Jazyk: |
angličtina |
| Zdroj: |
Organic & biomolecular chemistry [Org Biomol Chem] 2017 Oct 31; Vol. 15 (42), pp. 8883-8887. |
| DOI: |
10.1039/c7ob02391j |
| Abstrakt: |
We present the first cryptophane-based "turn-on" 129 Xe NMR biosensor, employing a peptide-functionalized cryptophane to monitor the activation of calmodulin (CaM) protein in solution. In the absence of CaM binding, interaction between the peptide and cryptophane completely suppresses the hyperpolarized 129 Xe-cryptophane NMR signal. Biosensor binding to Ca 2+ -activated CaM produces the expected 129 Xe-cryptophane NMR signal. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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