Structural and Functional Analyses of PAS Domain Interactions of the Clock Proteins Drosophila PERIOD and Mouse PERIOD2 (original) (raw)
Figure 6
Analytical Gel Filtration and Ultracentrifugation of mPER2
(A) Analytical gel filtration of mPER2 interface mutants. Wild-type, W419E, I427E, and F415E mutant versions of mPER2[128–473] were analysed on a HiLoad Superdex 200 10/30 gel filtration column. The elution positions of the crystallized mPER2[170–473] fragment as well as the marker proteins Ovalbumin and Apotransferrin are indicated.
(B) A typical sedimentation equilibrium experiment of dPER[128–473] wild-type at a single concentration (out of four). Data of other fragments and mutants were of comparable quality.
(C) Summary table of analytical ultracentrifugation of mPER2 variants. _K_D = 1/_K_A.
dof, degrees of freedom; fix, molar mass fixed to the expected value. 95% confidence intervals are given in brackets.