| dc.description.abstract | Protein interactions and kinetics can explain a proteins functions and activity. Protein interactions can be studied by a variety of high- and low-resolution methods. Native MS, an MS based technique where proteins native conformation and interactions are conserved, is a valuable tool to identify and quantify protein interactions. Unlike other methods, native MS does not require labelling for identification and qualification of different species in a sample, which makes it suitable for the analysis of proteins that are extracted from patient material. Additionally, native MS is particularly useful when analysing heterogenous samples. This review focusses on recent innovations to extent the native MS toolbox for the study of protein interactions. The showcased innovations, which are both online and offline, allow for extended usage of native MS, for example for the analysis of (thermo)dynamic properties. Also sample preparation and fragmentation innovations are discussed. Although innovation is rapid and there seems to be no limit, we believe that the current native MS toolbox can be exploited for the functional analysis of heterogenous samples, for example caused by post translational modifications or a mix of competitive binding partners. | |
