Matches in Ubergraph for { <https://frink.apps.renci.org/.well-known/genid/B9e4f500bdb6ef4f94acc5e87c0037fd6> ?p ?o ?g. }
Showing items 1 to 5 of
5
with 100 items per page.
- B9e4f500bdb6ef4f94acc5e87c0037fd6 hasDbXref "PMID:7708014" @default.
- B9e4f500bdb6ef4f94acc5e87c0037fd6 type Axiom @default.
- B9e4f500bdb6ef4f94acc5e87c0037fd6 annotatedProperty IAO_0000115 @default.
- B9e4f500bdb6ef4f94acc5e87c0037fd6 annotatedSource MI_0017 @default.
- B9e4f500bdb6ef4f94acc5e87c0037fd6 annotatedTarget "Proteins contain endogenous fluorophores such as tryptophan residue and heme or flavins groups. Protein folding and protein-protein interaction can be studied by monitoring changes in the tryptophan environment detected by changes in its intrinsic fluorescence. Changes in the fluorescence emission spectrum on complex formation can occur either due to a shift in the wavelength of maximum fluorescence emission or by a shift in fluorescence intensity caused by the mixing of two proteins. The interaction of two proteins causes a shift in the fluorescence emission spectrum relative to the sum of the individual fluorescence spectra, resulting in a difference spectrum [F (complex)-2 F (sum)], which is a measurable effect of the interaction. Loss of fluorescence signal from a substrate can be used to measure protein cleavage." @default.