Quartz 4

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Created Apr 10, 2026Modified Apr 21, 2026

The framework region of an antibody variable region is the core immunoglobulin domain.

Antibody affinity can be improved by stabilization
Antibody developability predictions are relatively stable to single point mutations
Antibody humanization
Antibody sequence similarity is not correlated with developability similarity
CDR3 mediates heavy-light chain pairing preferences by making contacts to framework residues
CUMAb
CabBCII-10 is a universal nanobody framework capable of accepting diverse CDRs
Conformational entropy in antibodies decreases during affinity maturation
Heavy and light chains of de novo designed antibodies with the same framework and binding mode can be exchanged
Inverse folding of CDRs benefits from span masking during training
Most camelid-derived nanobodies have high sequence identity with human IGHV3
Nanobodies
Nanobody FR2 is more hydrophilic than that of antibodies
Nanobody framework residues more likely to be part of paratope than those of antibodies
Net charge of CDRs strongly predicts nonspecific binding
Optimal scaling of antibody LMs improves prediction of masked CDRH3 residues but not framework residues
Wildtype antibody frameworks can accommodate CDRs that bind to virtually any target

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