We measured the flash-induced absorption anisotropies of mutant bacter
iorhodopsin (bR), D96N, in the purple membrane suspension, The measure
d anisotropy decay at 410 nm differed from that at 570 Mn. These wavel
ength-dependent anisotropies show that the motion of absorption dipole
of non-excited bR is faster than that of M-intermediate, The motion o
f non-excited bR is considered as the rotational motion of whole prote
in in the purple membrane, This fact suggests that the photo-excitatio
n induces the conformational change of the protein and/or the inter-pr
otein interaction within the membrane, which prevents the motion of M-
intermediate.