Bifurcation analyses on feedback loops indicate that multiple feedback loops are coordinated to modulate sporulation efficiency.
These results confirm that the loop-flipping frequency of a given loop depends strongly on the number of charges on that loop, indicating that charge mutations can impact the determination of the slowest-flipping loop.
However, MrkH116-end loses the c-di-GMP binding affinity, which indicates that the connecting loop between two β-barrels is crucial for c-di-GMP binding.
Although x-ray structures of antithrombin, free and complexed with heparin, have suggested that exposure of a reactive proteinase binding loop is a key feature of conformational activation, mutagenesis of reactive loop residues indicates that the function of this structural change is not to present an optimal loop sequence to target clotting proteinases.
In this way, our structure models indicate that tight ADP binding would be an inherent property of detached kinesin, where the switch loops are free to adopt an open conformation.
A fourth mAb with a longer CDR2 loop was not affected by mutation of residue 57, indicating that CDR2 domain length may alter the binding interface and lead to the involvement of other residues in protein A binding.
Ablation of the terminal loop of pre-let-7a-1 also reduced the binding frequency, indicating that TUT7 recognizes both the overhang and the terminal loop.
However, our results suggest that Cry1Aa activity does not depend on conserved amino-acid sequences in loops, indicating an unusual binding character compared with other proteins.
The deletions ΔSL1 (Δ7–34) or ΔSL3 (Δ246 255, Δ246–255) did not reduce eEF1A1 binding to the 3′UTR significantly, whereas the deletions in stem-loop 2 (Δ151 158–93, Δ151–158) abolished eEF1A1 binding, indicating that this region was the primary interacting site for eEF1A1.
The perturbed residues upon Cbp binding indicate that βB-βC, βD and βD-βE loops of L-SH2 undergo significant conformational change.
