The number of such elementary loops is equal to the number of inefficient options.
Elementary functional loops (EFLs), closed loops with one or few catalytic residues, are, in turn, units of the protein function.
Functionally, the notion of elementary functional loops (EFLs), closed loops possessing the residues important for binding, activation, and catalysis has been introduced [ 10, 23, 24].
Thus the ground part of the elementary leakage loop that carries a current j(x′ dx′ can be replaced with a vertical upward current at x = y = 0, 0 ≤ z ≤ ∞ and a vertical downward current at x = x′, y = 0, 0 ≤ z ≤ ∞.
The magnetic field due to an elementary leakage loop has exactly the same form as equations (11)–(13) of Pirjola et al. (2007), except that j = j(x′) = kx′ is a function of x′ i.e. (14) (15) (16) The integration of Eqs.
We relied here on the concept of elementary functional loop (EFL) as a presumed basic unit of the protein function.
The elementary functional loop 515 with the signature -Rx [TS] × [TS]AxxADx 6 PG[TS]D- is likely responsible for the MGD-binding.
Figure 5 shows an example of the elementary functional loop representing the profile 45 in RecA-superfamily, where its function is the ADP binding.
Figure 5 contains the example of the EFL corresponding to the profile 280, where an elementary functional loop from a Lysil-tRNA synthetase is shown together with substrates Lysine and ATP.
The elementary functional loop containing this characteristic signature is a part of the active site in aaRS class I, where the second lysine stabilizes the aminoacyl-adenylate. Figure 5 shows the structure of the corresponding EFL.
The leakage current J x) gives the total amount of current in the elementary leakage loops whose width is larger than or equal to x.
