Synthesis of Bi-Sr-Ca-Cu-O Wires for Perspective Applications

Consideration of Binding Kinetics in the Design of Stapled Peptide Mimics of the Disordered Proteins Eukaryotic Translation Initiation Factor 4E-Binding Protein 1 and Eukaryotic Translation Initiation Factor 4G

“…While binding affinities of IDPs/IDRs have been typically shown to correlate with k a , 57 a recent report found that this is not always the case. 58 Using stoppedflow fluorescence spectroscopy, the binding affinities of disordered peptide mutants for PDZ domains were found to correlate with changes in k d rather than k a because of side-chain interactions that occurred late and cooperatively after the rate-limiting barrier. 58 Deviations between the 4E-BP1 and eIF4G peptides were observed primarily at 30 °C (Tables S2 and S3).…”

“…58 Using stoppedflow fluorescence spectroscopy, the binding affinities of disordered peptide mutants for PDZ domains were found to correlate with changes in k d rather than k a because of side-chain interactions that occurred late and cooperatively after the rate-limiting barrier. 58 Deviations between the 4E-BP1 and eIF4G peptides were observed primarily at 30 °C (Tables S2 and S3). Thus, at higher and more physiologically relevant temperatures, 4E-BP1 binding seems to be preferred possibly because of its greater complementarity to eIF4E and its increased population of bioactive conformation (vide supra).…”