Matches in Ubergraph for { <https://frink.apps.renci.org/.well-known/genid/B6a41a6b9d2b5f2f09fa84fc5e989f3e4> ?p ?o ?g. }
Showing items 1 to 5 of
5
with 100 items per page.
- B6a41a6b9d2b5f2f09fa84fc5e989f3e4 hasDbXref "PMID:7708014" @default.
- B6a41a6b9d2b5f2f09fa84fc5e989f3e4 type Axiom @default.
- B6a41a6b9d2b5f2f09fa84fc5e989f3e4 annotatedProperty IAO_0000115 @default.
- B6a41a6b9d2b5f2f09fa84fc5e989f3e4 annotatedSource MI_0017 @default.
- B6a41a6b9d2b5f2f09fa84fc5e989f3e4 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.