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- MI_0053 IAO_0000115 "Because of the long lifetimes of excited fluorescent molecules (nanoseconds), fluorescence can be used to monitor the rotational motion of molecules, which occurs on this timescale. This is accomplished experimentally by excitation with plane-polarized light, followed by measurement of the emission at parallel and perpendicular planes. Since rotational correlation times depend on the size of the molecule, this method can be used to measure the binding of two proteins because the observed polarization increase when a larger complex is formed. A fluorescence anisotropy experiment is normally carried out with a protein bearing a covalently added fluorescent group, which increases both the observed fluorescence lifetime of the excited state and the intensity of the fluorescent signal. Residue modification can be assessed by addition of an antibody which binds to the modified residue and alters the molecular weight of the complex. A variation of this technique has been used to show interaction of a DNA binding protein with another protein. In this case the DNA rather than protein is fluorescently labelled." @default.
- MI_0053 normalizedInformationContent "100" @default.
- MI_0053 referenceCount "1" @default.
- MI_0053 hasExactSynonym "FPS" @default.
- MI_0053 hasExactSynonym "Fluorescence anisotropy" @default.
- MI_0053 hasExactSynonym "fps" @default.
- MI_0053 hasOBONamespace "PSI-MI" @default.
- MI_0053 id "MI:0053" @default.
- MI_0053 inSubset PSI-MI_slim @default.
- MI_0053 type Class @default.
- MI_0053 isDefinedBy mi.owl @default.
- MI_0053 label "fluorescence polarization spectroscopy" @default.
- MI_0053 subClassOf MI_0000 @default.
- MI_0053 subClassOf MI_0001 @default.
- MI_0053 subClassOf MI_0013 @default.
- MI_0053 subClassOf MI_0045 @default.
- MI_0053 subClassOf MI_0051 @default.
- MI_0053 subClassOf MI_0053 @default.