Table 2.
Fluorescence maximum emission wavelengths of StI W111C monomer and homodimer forms.
| Fluorescence Emission Parameters In Solution | ||||
|---|---|---|---|---|
| λmax (nm) Trp + Tyr residues | ||||
| Proteins | −AA−2ME | +AA−2ME | −AA+2ME | +AA+2ME |
| Monomer | 334 ± 0.5 | 332 ± 1.0 | 334 ± 0.5 | 331 ± 0.6 |
| Homodimer | 334 ± 0.6 | 332 ± 1.5 | 334 ± 0.5 | 331 ± 0.7 |
| λmax (nm) Tyr residues | ||||
| Proteins | −AA−2ME | +AA−2ME | −AA+2ME | +AA+2ME |
| Monomer | 319 ± 0.6 | 319 ± 1.0 | 322 ± 2.0 | 316 ± 1.0 |
| Homodimer | 322 ± 1.5 | 323 ± 1.0 | 316 ± 2.0 | 317 ± 2.0 |
| λmax (nm) Trp residues | ||||
| Proteins | −AA−2ME | +AA−2ME | −AA+2ME | +AA+2ME |
| Monomer | 339 ± 0.6 | 337 ± 1.5 | 338 ± 0.6 | 333 ± 0.6 |
| Homodimer | 339 ± 0.5 | 338 ± 1.0 | 338 ± 0.5 | 334 ± 0.7 |
Fluorescence maximum emission wavelengths (λmax) for Trp and Tyr residues were calculated from spectra of monomer and homodimer oligomeric forms in solution (Fig. 6). Homodimer and monomer were analyzed by pre-incubating with 15 mM 2-mercaptoethanol (+2ME) during 24 h and without pre-incubation (−2ME). Fluorescence emission from oligomeric forms were also quenched with 300 mM acrylamide (+AA) and analyzed in the absence of quencher (−AA).