(i) Antibody variants were tested for binding to soluble EBOV, BDBV (j), or SUDV (k) GP ectodomain immobilized on ELISA plates.
Each peptide was tested for binding to HLA-A2 in a HLA-A2 stabilization assay.
(a) 29 mice sera displaying the highest signals against OLP 162 peptide were tested for binding against a collection of OLP 162-alanine mutants.
The resulting peptide (PEPHC1) was synthesized and tested for binding to EGFRvIII and EGFR.
These compounds were tested for binding to the XIAP-BIR3 and ML-IAP BIR using a fluorescence polarization assay.
The resulting eightfold mutant, CaM_8, was constructed and tested for binding to a set of seven CaM target peptides.
A set of Gα12 mutations with systematic replacement of six amino acids with NAAIRS was tested for binding to the PC1 C-terminus in GST pulldowns.
Analogs were tested for binding to I-Aq using a competitive binding assay and selected analogs were administered to arthritic mice.
Several CaM variants were experimentally constructed and tested for binding to the CaMKII and CaN peptides using the surface plasmon resonance technique.
Nine peptides, named CB1 to CB9, were identified, synthesized in a cyclic and soluble form and tested for binding to recombinant soluble CD4.
Mutant profilins were tested for binding to poly-l-proline and the VASP and mDia1 peptides, and the F139A mutant bound proline-rich ligands with near-native affinity.
