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Because many methods are not designed to infer self-interactions or interaction direction we disregard directed edges and self-interactions.
The centroid of the corresponding interacting atoms is defined as the main interaction direction starting point.
Then, for each residue that is interacting with this particular ligand, the main interaction direction starting point is calculated and stored as the anchor point.
Each residue in a complex has a main interaction direction with a defined starting point.
The term anchor point is defined as the global coordinate for the starting point of the main interaction direction of a residue on the ligand side.
A spot has an associated interaction direction which indicates hydrogen or lone pair orientation, and thus, the potential location of a hydrogen-bond counterpart.
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This is caused by the difference in the interaction patterns and the minimization of the deviation between the optimal interaction directions of the ligand and the real interaction directions given by the globally set amino acid positions.
The adjustment of the residue structure diagram is done by superimposing the global main direction of the ligand and the inverted resultant direction of all individual residue interaction directions of the individual complexes.
This has the benefit of a finite number of possible interaction directions r ˆ, in particular when θ crit = 1, for which the coefficients Θ n m ( r ˆ ) could be pre-computed.
We can see two interaction directions: From the Persona to the Self i.e., to the user with all the experiences, sensors, memory, thinking systems, heuristics, etc.; and From the Self to the Persona i.e., to a simplified view of the user, specifically made for the UI and the system being studied.
These include three cases of protein-compound-protein (PCP) interaction processing, reversing binding interaction directions of seven edges and processing of two group nodes.
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