Fig. 2
From: Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A
Binding affinity of wild type and mutant CypA for CA and cross-linked CA hexamers. Equilibrium analysis of surface plasmon resonance (SPR) curves of CypA binding on surfaces modified with CA K158C (reacted with a maleimide derivative of biotin) or cross-linked CA A14C/E45C/W184A/M185A hexamers (reacted with an NHS ester derivative of biotin). The SPR curves are shown in Additional file 1: Figure S2. a SPR response at equilibrium as a function of CypA concentration and fit of a binding model to the data (black line) to obtain the dissociation constant of the CypA interaction. b Equilibrium dissociation constants (KD) determined for wild type CypA and mutant interacting with CA and CA hexamers from the single experiments shown in A