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. Author manuscript; available in PMC: 2008 Jun 8.
Published in final edited form as: J Mol Biol. 2007 Jan 27;369(3):696–709. doi: 10.1016/j.jmb.2007.01.060

Table 1.

Affinity constants (Kds) obtained for the B2.1 sequence as a synthetic peptide and as a fusion at the N-terminus of the maltose binding protein of E. coli (B2.1-MBP) as determined by a kinetic exclusion assay (KinExA) and surface plasmon resonance (SPR).

Reactants1 Method Sequence Kd (M)
B2.1 peptide- IgG2 KinExA NH3-HERSYMFSDLENRCIAAE-Orn(biotin)-KK-NH2 2.5 × 10−6
B2.1 peptide- Fab SPR, Equil/soln NH3-HERSYMFSDLENRCIAAE-Orn(biotin)-KK-NH2 5.0 × 10−6
Fab b12-B2.1 SPR, Steady-state NH3-HERSYMFSDLENRCIAAE-Orn(biotin)-KK-NH2 6.9 × 10−6
IgG b12-B2.1/MBP KinExA NH3-HERSYMFSDLENRCIAAEE-MBP 6.0 × 10−8
IgG b12-B2.1/MBP SPR, Kinetic NH3-HERSYMFSDLENRCIAAEE-MBP 2.0 × 10−8
1

For the kinetic and the steady-state methods in SPR, the first of the reactants in each pair listed is the one immobilized on the sensor chip, the second is the in-solution analyte that is passed over the immobilized ligand.

2

Previously published result (21).