Multi-user quipament approved in grant 2014/17264-3: 2D nanoUPLC system

• Grant number: 17/14476-8
• Support Opportunities: Multi-user Equipment Program
• Start date: August 01, 2017
• End date: July 31, 2024
• Field of knowledge: Biological Sciences - Biochemistry - Chemistry of Macromolecules
• Principal Investigator: Fabio Cesar Gozzo
• Grantee: Fabio Cesar Gozzo
• Host Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
• Associated research grant: 14/17264-3 - New frontiers in structural proteomics: characterizing protein and protein complex structures by mass spectrometry, AP.TEM
• EMU web page: Página do Equipamento Multiusuário não informada
• Type of equipment: Caracterização de Materiais - Análises Químicas - Cromatrografia líquida
• Manufacturer: Fabricante não informado
• Model: nanoUPLC 2D

Abstract

The study of protein interactions is an important field to understand protein functions. This is, however, one area of great experimental difficulties due to inherent complexity of proteins and peptides. High resolution structural tools (i.e. X-Ray diffraction and Nuclear Magnetic Resonance are the de facto methods for these studies. However, most proteins and protein complexes are not amenable to have their structures solved by these techniques, requiring the use of other alternative methods to structurally characterize proteins and proteins complexes. Mass Spectrometry (MS) is an attractive technique for characterization of proteins due to its intrinsic characteristics, such as sensitivity, speed and broad applicability. Our group have been working on this field in the last 6 years (MS (da Silva et al, 2013, Fioramonte et al., 2012; Santos et al., 2011a; Santos et al., 2011b; Santos et al., 2010; Iglesias et al., 2010; Iglesias et al., 2009). In this project, we intend to use MS to characterize the structure of proteins and protein complexes. These experiments will be performed to obtain distance constrains from cross-linking experiments along with data from hydrogen/deuterium experiments and ion mobility and all these data will be used in a combined fashion to generate structural models of protein and complexes of biological interest. (AU)