Mass spectrometry is the dominant technology in the field of proteomics, enabling the indentification and quantification of cellular proteins and their modified forms.
Instruct has 5 centres offering Mass Spectrometry across Europe. Navigate the map and click on the pins to discover centres near you.
Since its beginnings in studying the mass of isotopes in the early 1900s, Mass Spectrometry (MS) has evolved such that molecules containing hundreds of thousands of atoms can now be accurately and sensitively measured. However MS is not limited to molecules held together by covalent chemical bonds and can be used to examine fragile protein assemblies in the gas phase.
MS within Instruct therefore provides a rapid and sensitive means for assessing the quaternary organisation of proteins. It is widely applicable, including to assemblies as large as viruses, containing intrinsically disordered regions, associated with membranes, or populating a range of oligomeric states. The state-of-the-art enables the determination of inter-subunit connectivity, protein shape and topology, and equilibrium dynamics. Combining this ability to inform on the quaternary structure level with analysis of the individual protein chains renders MS a vital bridge between proteomics and structural biology.
Native mass spectrometry (MS) is a tool that allows the structural investigation of protein complexes. It will not provide a structural model in atomic detail, but the sensitivity, speed, selectivity, unlimited mass range and accuracy of the analysis provides important advantages over other techniques. It’s sensitivity allows the investigation of endogenous protein complexes, and another major benefit of the method is that it can simultaneously analyze several species in one spectrum. If there is a heterogeneous population of protein complexes present in one sample, the one of interest can be specifically isolated for further studies.
Within this research field electrospray ionization is the most popular technique to ionize the proteins/protein complexes of interest. It is a gentle ionization method allowing the preservation of quaternary protein structures. Normally the protein complex is sprayed from a volatile buffer, compatible with the electrospray process.
A range of mass spectrometric approaches can be applied to investigate the biological systems. The exact mass of proteins can be determined, but also the stoichiometry of an assembly, its stability, dynamical behavior, conformation, subunit interaction sites and topological arrangement of the individual proteins within a complex.
Native ion mobility mass spectrometry (IMMS), is a rather new tool in structural biology. Complementary to the separation of the ions based on mass, they are also separated according to their physical size. Typically, ions with a larger cross section (volume) exhibit longer drift times in the gas-filled ion mobility chamber. Therefore, IMMS can reveal direct information regarding the shape and conformation of a protein complex. Up to now several IMMS studies have indicated that solution phase structures are often largely retained in the gas-phase, making this method potentially a valuable new tool in structural biology. The size measurements of the ions obtained by IMMS can then be used with computational modeling to generate refined structural models for the protein complex in question.
Mass spectrometry is the dominant technology in the field of proteomics, enabling the indentification and quantification of cellular proteins and their modified forms. In Instruct we correlate our structural insights into protein assemblies with this fundamental information about the individual chains. We offer access to state-of-the-ar proteomics facilities, including identification and quantification of proteins, peptides and post-translational modifications.