The Molecular Structure and Function Laboratory determines protein structure and analyzes protein modifications through collaborations with IBR investigators and extramural scientists, using a Waters Q-Tof Micro tandem mass spectrometer (MS/MS) and NanoAcquity liquid chromatography (LC) system.
Over 1,600 individual samples have been analyzed using a wide range of methods since the facility began operations. The majority of the samples have been analyzed by LC-MS/MS to identify disease-associated proteins in trypsin-digested samples isolated by the investigators from 1-D or 2-D PAGE gels. Other analyses have included confirmation of the structure of synthetic peptides and purified proteins, analyses of purified proteins for phosphopeptides, dimethylarginine, methionine oxidation or other post-translational modifications, analyses of tissue fractions for known proteins or peptides, and surveys of disease-related proteins in fractionated preparations, including immunoprecipitates, from tissues or cultured cells.
A major goal of this laboratory is to identify proteins or protein modifications that are relevant to the causes of various developmental disabilities. Once identified, the proteins or protein-specific modifications are further studied to determine their role in the causation of disease, their applicability as diagnostic markers, and their relevance to possible treatment regimes. By assisting in the critical first step of identifying disease-specific markers, the laboratory helps investigators increase their understanding of the disease of interest. The laboratory also facilitates more advanced studies of disease, in which understanding of the disease process may require analysis of specific aspects of protein expression, modification, or degradation.