Thread: NMR paper The detection of proline isomerase activity in FK506-binding protein by two-dimension
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Default The detection of proline isomerase activity in FK506-binding protein by two-dimension
The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.

Related Articles The detection of proline isomerase activity in FK506-binding protein by two-dimensional 1H NMR exchange spectroscopy.

Biochem Biophys Res Commun. 1990 Aug 31;171(1):445-50

Authors: Justice RM, Kline AD, Sluka JP, Roeder WD, Rodgers GH, Roehm N, Mynderse JS

1H NMR assignments of the trans and cis isomers of succinyl-Ala-Ala-Pro-Phe-p-nitroanilide were accomplished by two-dimensional NMR techniques. Conformational exchange between the cis and trans isomers was not detected in the two-dimensional exchange spectra (NOESY) until catalytic amounts of FK506-binding protein (FKbp) were added. The addition of FK506 to the enzyme-substrate solution inhibited the enzyme and removed the substrate exchange peaks.

PMID: 1697463 [PubMed - indexed for MEDLINE]



Source: PubMed
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