 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 3]](ba5100fig3mag.jpg)
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Figure 3
The use of FRET to determine the correct dimer structure for α1-antitrypsin (Sivasothy et al., 2000  ). (a) Models showing three possible dimer structures: I, II and III. The residues upon which fluorophores are attached are shown in dimer I. (b) The fluorescence of a donor fluorophore in the presence of an acceptor fluorophore is measured under conditions that promote and disrupt polymerization. FRET results in a decrease in the fluorescence from the donor fluorophore. A range of FRET signals are measured for proteins with fluorophores at different positions on the surface of α1-antitrypsin. These are then used to model the structure of the dimer. The correct dimer is dimer III. |
![[Figure 3]](ba5100fig3.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
