Nanomolar Protein–Protein Interaction Monitoring with a Label-Free Protein-Probe Technique
Salla Valtonen, Emmiliisa Vuorinen, Taru Kariniemi, Ville Eskonen, John Le Quesne, Martin Bushell, Harri Härmä, Kari Kopra
Abstract
chelate, and it has already been applied to monitor protein structural changes and small molecule interactions at elevated temperatures. Here, the applicability of the protein probe technique was demonstrated by monitoring single-protein pairing and multiprotein complexes at room and elevated temperatures. The concept functionality was proven by using both artificial and multiple natural protein pairs, such as KRAS and eIF4A together with their binding partners, and C-reactive protein in a complex with its antibody.
Topics & Concepts
ChemistryFörster resonance energy transferProtein–protein interactionSurface plasmon resonanceTarget proteinFluorescenceBiophysicsSmall moleculePeptideProtein GCombinatorial chemistryNanotechnologyBiochemistryNanoparticleAntibodyPhysicsQuantum mechanicsBiologyImmunologyMaterials scienceGeneBiotin and Related StudiesViral Infectious Diseases and Gene Expression in InsectsMonoclonal and Polyclonal Antibodies Research