Summary
Introducing many arginine residues into CDRH3 has been suggested to increase polyreactivity, presumably by increasing CDRH3 flexibility. MD simulations show in one case that nearby arginines are repulsed by one another and increase flexibility (1).
See also
- Conformational entropy in antibodies is inversely proportional to antigen affinity
- CDRH3 conformational rigidity reduces cross reactivity
- Antibody thermostability decreases during affinity maturation, up to a threshold
- Net charge of CDRs strongly predicts nonspecific binding
1.
Fernández-Quintero ML, Loeffler JR, Kraml J, Kahler U, Kamenik AS, Liedl KR. Characterizing the Diversity of the CDR-H3 Loop Conformational Ensembles in Relationship to Antibody Binding Properties. Frontiers in Immunology. 2019;9. Available from: https://doi.org/10.3389/fimmu.2018.03065