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Note that the computational load of SC-PRS M(4) relies on the resulting two complementarity problems, which are computationally expensive, especially for large-scale problems.
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Shark heavy chain antibody, also called new antigen receptor (NAR), consists of one single Variable domain (VH), containing only two complementarity-determining regions (CDRs).
Shark sdAbs contain four conserved frame regions (FRs) and two complementarity-determining regions (CDRs), making them the smallest (~12 kD) Ig-based recognition units with full capacity for antigen binding affinity and specificity.
Finally, these two contributions are brought together in The Complementarity-Capability Matrix, where we propose seven complementarity strategies and resources and capabilities necessary to achieve them.
The VH of avelumab dominates the binding to hPD-L1 by all three complementarity determining regions (CDR) loops, while VL contributes partial contacts by the CDR1 and CDR3 loops, leaving VL CDR2 without any binding to hPD-L1 (Fig. 2B left).
The epitope is composed of a linear array of nine residues (Arg138, His141 Arg148) located at the tip of a helix turn helix motive which protrudes away from the globular core and fits tightly into the deep surface pocket formed by the residues from the six complementarity determining regions (CDRs) of the Fab.
The latter include six complementarity determining regions (CDRs) which constitute the antigen (Ag) binding-site.
Five complementarity groups, i.e. recognizing different regions of Cry1Ab protein, were characterized, one of which was specific to the C-terminal part of the protoxin [30].
Each VH and VL domain contains three complementarity determining regions (CDRs).
More than 20 million complementarity determining region (CDR) 3 sequences were analyzed.
The V regions of each of these chains comprise three complementarity determining regions (CDRs) separating four more conserved framework (FW) regions [ 1].
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