Matches in Ubergraph for { <http://purl.obolibrary.org/obo/MI_0017> ?p ?o ?g. }
Showing items 1 to 16 of
16
with 100 items per page.
- MI_0017 IAO_0000115 "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.
- MI_0017 normalizedInformationContent "100" @default.
- MI_0017 referenceCount "1" @default.
- MI_0017 hasExactSynonym "fluorescence spectr" @default.
- MI_0017 hasOBONamespace "PSI-MI" @default.
- MI_0017 id "MI:0017" @default.
- MI_0017 inSubset PSI-MI_slim @default.
- MI_0017 type Class @default.
- MI_0017 isDefinedBy mi.owl @default.
- MI_0017 label "classical fluorescence spectroscopy" @default.
- MI_0017 subClassOf MI_0000 @default.
- MI_0017 subClassOf MI_0001 @default.
- MI_0017 subClassOf MI_0013 @default.
- MI_0017 subClassOf MI_0017 @default.
- MI_0017 subClassOf MI_0045 @default.
- MI_0017 subClassOf MI_0051 @default.