Effect of multiple symmetries on the association of R67 DHFR subunits bearing interfacial complementing mutations
Protein Sci
Dam and Blondel 13 (1): 1.
Supplemental Research Data
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The supplementary material contains data that complete the establishment of the association model for the heterotetramers of R67 DHFR. They were collected separately to allow a more concise presentation.
Figure S1 A&B, similar to Figure 1 A&B with titration curves for other pairs of mutations.
Figure S2, possible reactions without heterodimers.
Figure S3 A&B, IEF PAGE showing the formation of heterodimers and the effect of incubation time and temperature.
Figure S4 A&B, Inhibition by a third party mutant showing the formation of
heterodimers.
Figure S5, identification of the relevant reactions among possible ones.
Figure S6, illustration of data analysis.
Table S1, effect of v;- values on the fitting of analytical ultracentrifugation data, robustness assessment.
Annex 1, effect of the incubation conditions on the association regime of pair (59A)2+(62L)2 showing that protomer redistribution, although very slow, can occur for that pair.
Annex 2, formalization of the effect of the protomer stability on the association showing that there should be no symmetry propensity.
References.
