National Resource for Mass Spectrometric Analysis of Biological Macromolecules
From BTRR
Overview
The resource develops new mass spectrometric tools for studying biological processes involving proteins: the basic research focuses on investigations of techniques for volatilizing and ionizing proteins. It also designs and constructs mass spectrometric-based method to assist in the solution of challenging biological problems. The resource applies these tools to the solution of biological problems that involve, for example, the rapid identification of proteins, the elucidation of posttranslational modifications, and the definition of sites of functional interaction between biomolecules.
Current Research
Investigations of the matrix-assisted laser desorption ionization (MALDI) and electrospray ionization processes and the gas-phase fragmentation of biopolymers. Improved instrumentation for rapid, sensitive fragmentation analysis of peptides for protein identification. Improved instrumentation for ultra high-sensitivity detection of phosphopeptides. The origin of the "chemical noise" background and means for reducing it or its effects. Improved methodologies for studying protein interactions: ultimate goals include detecting single molecules of interest and making a map of all protein interactions within a cell, both stable and transient. Improved methods for studying protein phosphorylation: ultimate goal is to define the "phosphoproteome" of an organism. Development of a tool set for differential proteomics research that includes methods to accurately quantify changes in the levels of proteins and protein modifications. Development of mass spectrometry (MS) as a tool for the atomic resolution structure analysis of proteins, including integral membrane proteins and ion channels. Development of mass spectrometric informatics tools for analysis of the proteome and tools for annotating the human genome using mass spectrometric information.
