Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody.

By K. Midelfort, H. H. Hernandez, S. Lippow, Bruce Tidor, Catherine L. Drennan, K. Wittrup. 2004

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Engineered antibody fragments and the rise of single domains (2005, background): “In a striking example, a single designed point mutation increased hapten-binding affinity of an scFv fragment by 1,800-fold (ref”
Selecting and screening recombinant antibody libraries (2005, background): “, through mutations in the framework region—parts of the variable regions that are not hypervariable—that modulate CDR loop flexibility or affect the orientation of the V H and V L domain”
Repertoire Analysis of Antibody CDR-H3 Loops Suggests Affinity Maturation Does Not Typically Result in Rigidification (2017, background): “60 Å) and thermodynamic measurements 526 suggested that the affinity improvement was achieved primarily through the enthalpic interactions 527 with subtle conformational changes (67).”
AbDesign: an algorithm for combinatorial backbone design guided by natural conformations and sequences (2015, background): “3, Protein Data Bank (PDB) entry 1X9Q, a high-expression, high-affinity anti-fluorescein antibody,78 although the choice of template is arbitrary). k variable light chains were not included in the current database because of the relatively small number of available structures in the PDB (1300…”