Table 1

: Fluorescence and dissociation of wild-type versus mYFPs without lipid modifications. Dissociation constantK d (mM) derived from the association constant (K a) was measured by sedimentation equilibrium analytical ultracentrifugation. Variance (goodness of fit) was determined by global analysis with a nonlinear least-squares algorithm in the software provided by Beckman. Each value is statistically significant.

MutationQuantum yieldExtinction coefficient (M−1cm−1)KdVariance
Wild type0.6767,0000.111.25E-3
L221K0.6764,0009.71.35E-3
F223R0.5365,0004.81.48E-3
L221K/F223R0.6859,0002.44.60E-4
A206K0.6279,00074* 6.65E-4*
  • * Due to the extreme monomeric nature of this protein it was difficult to determine an accurate dissociation constant for a hypothetical dimer.