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The binding interactions of three gemini surfactants having different spacer groups (12-4-12, 12-8-12, and 12-4(OH)-12)with a high concentration (150 mu M)of bovine serum albumin (BSA)at various regions of binding isotherms have been studied by means of steady-state fluorescence and fluorescence anisotropy, time-correlated single-photon counting fluorescence of trans-2-[4-(dimethylamino)styryl]benzothiazole, small-angle neutron scattering (SANS), and dynamic light scattering (DLS)measurements. The fluorescence resonance energy transfer phenomenon between the twisted intramolecular charge transfer fluorescent molecule, trans-2-[4(dimethylamino)styryl] benzothiazole as an acceptor, and tryptophan 213 (Trp-213) of BSA as a donor has been successfully used to probe the binding interactions of gemini surfactants with protein at all regions of binding isotherms. The increasing order of energy transfer efficiency at a higher concentration range of surfactants is 12-8-12 > 12-4-12 > 12-4(OH)-12. Stronger binding of micelles of gemini surfactant molecules having a comparatively more hydrophobic spacer group with the hydrophobic segments of the protein results in closer approach of trans-2-[4-(dimethylamino)styryl] benzothiazole molecules solubilized in micelles to Trp-213. The average excited-state lifetimes become shorter with a trend of increase in contribution from the fast component and decrease in contribution from the slow component to the decay with increasing concentration of a surfactant. The nonradiative rate constant of trans-2-[4-(dimethylamino)styryl] benzothiazole increases with increasing concentration of a surfactant because the average microenvironment around it in protein-surfactant aggregates is more polar as compared to that in native protein. SANS and DLS measurements were carried out for the study of the structural deformations in the protein, on enhancement of the concentration of the gemini surfactants. The necklace and bead model has been used