Assuming that pairs of nodes interacting with the central ego in a similar way are more prone to be connected, the score of the pair ((i,j) ) is then computed from the scalar product of these weight vectors: s_{mathrm{pr}}(i,j) = frac{(w_{A} e,i) cdot w_{A} e,j) + w_{B} e,i) cdot w_{B} e,j))}{W e)}.
Based on these results, and on the analysis of molecular dynamics simulations, we suggest that the phosphorylated regulatory segment of CaMKII interacts with the central hub of the holoenzyme and weakens its integrity, thereby promoting exchange.
Neuromodulatory systems originate in nuclei localized in the subcortical region of the brain and control fundamental behaviors by interacting with many areas of the central nervous system.
The efference copy is, however, not used to generate the ongoing motor activity, but can be used to predict the outcome of the motor command [24] [28] (information of efference copies interact at several levels of the central nervous system, and often modulate sensory processing; for reviews, see [34], [35]).
The observation of large inhibitor-induced changes at Arg5 and Phe20 suggests that Arg5 may interact directly with Phe20 of the central KLVFF sequence.
Additionally, the N-terminal area of the L19e protein directly interacts with the residues of the central bottom side of the GTS1 tunnel, leaving the central top side of the tunnel free as detailed in Figure 8B.
A total of ten copies of subunit c in yeast F-ATP synthase are found to associate into a ring structure that interacts with the foot of the central stalk subunits in the intact enzyme [ 7].
Most of the inhibitory region of cTnI is unobserved in cTnC·3Ca2+·cTnI31−210·cTnT183−288, but a similar region of sTnI is shown to have an extended conformation and interact with the central helix area of sTnC in the X-ray structure of the sTnC·4Ca2+·sTnI1−182·sTnT156−262 complex (8).
Clearly, whereas Bcl-2 exclusively interacts with the central domain of the IP3R, Bcl-Xl seems to interact with the C-terminal tail of the IP3R.
Chloramphenicol footprinting studies with specific nucleotides has revealed the binding sites 72, 73 to be on the 50S ribosomal subunit where chloramphenicol interacts with the central loop of 23S rRNA domain V to inhibit peptidyl transferase activity 68, 71, 72.
