Ontology highlight
ABSTRACT:
SUBMITTER: Riggle BA
PROVIDER: S-EPMC5681859 | biostudies-literature | 2017 Oct
REPOSITORIES: biostudies-literature
Riggle Brittany A BA Greenberg Mara L ML Wang Yanfei Y Wissner Rebecca F RF Zemerov Serge D SD Petersson E James EJ Dmochowski Ivan J IJ
Organic & biomolecular chemistry 20171001 42
We present the first cryptophane-based "turn-on" <sup>129</sup>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 <sup>129</sup>Xe-cryptophane NMR signal. Biosensor binding to Ca<sup>2+</sup>-activated CaM produces the expected <sup>129</sup>Xe-cryptophane NMR signal. ...[more]