The results from the compositions, i.e. the composed patterns and the split fragments of patterns not used by composition rules are returned to an input set of periodic patterns and step 3 is repeated.
Interaction of the two proteins brings the split fragments into close proximity, resulting in reassembly of the fluorescent protein.
DmsD interaction with TatB or TatC resulted in a ∼2-4-fold increase in the BiFC signal above background that was independent of the orientation of the split fragments (Fig. 6b).
To visualize protein interactions between soluble and transmembrane factors that participate in various steps of the Tat export process, we employed BiFC based on split fragments of enhanced yellow fluorescent protein (YFP).
Each of the split fragments of the Venus fluorescent protein was fused to the N-terminus or the C-terminus of AbdA and Exd.
This property explains that the complex formation between fusion proteins is generally stabilized by the association of split fragments, allowing the visualization of weak and transient interactions.
Generally speaking, the biologic functions of the complement system are mediated through the production of activation (or split) fragments, including C3a, C4a, and C5a.
Trees saved before the average standard deviation of split fragments converged to a value < 0.01 were discarded from the final sample.
