Comparison between results from pinch analysis and bridge analysis shows that the latter identifies supplementary solutions to save energy.
Therefore supplementary solutions for restoring lakes have been explored, including the capping of sediment P sources using a lanthanum (La -modified bentonite cLa -modifiede internal P loading and enhance the recovery process.
While the wild-type PDLP5 ectodomain behaves as a monomer in solution (Supplementary Figure 9), the mutant protein tends to aggregate in our biochemical preparations (Supplementary Figure 9) and display reduced structural stability in thermofluor assays (Supplementary Figure 10).
Gel filtration profiles also indicated that AcrIIA6 is a dimer in solution (Supplementary Fig. 3).
No complexation, however, between 2·2Cl and γ-CD was observed (Fig. 1b) in aqueous solution (Supplementary Figs 15−17).
Acid treatment with 10 M HCl likewise destroys the activity of lysozyme in solution (Supplementary Table S2).
However, size exclusion chromatography experiments show MCR1ΔTM is monomeric in solution (Supplementary Figure S2), leading us to conclude that this dimeric form is unlikely to be physiologically relevant.
Without Pt and Ni, the Al2O3 layer was not stable in KOH solution (Supplementary Fig. 7), and thus could potentially delaminate the metal overlayers, which would subsequently cause a rapid degradation of performance.
The dimer structure probably does not reflect the physiological form of the protein, because size exclusion chromatography showed that TM0415 is a monomeric protein in solution (Supplementary Fig. 3b).
Dynamic light scattering (DLS) analysis was carried out to study the interaction in solution (Supplementary Fig. S3): the proteins were first analyzed alone, resulting in a hydrodynamic radius of 4.2 nm and 6.2 nm for LOX-1 and NadA, respectively.
The residual enzyme activity observed at saturating BLIP concentrations is due to the fact that under these experimental conditions hybridization between the enzyme recruiter strand and BTA-DNA is not complete, leaving 25% of the enzyme free in solution (Supplementary Note 1).
