Medical Sciences Building, Room 351 Email: email@example.com
The FPF is the most common entry point for researchers requiring analysis of complex mixtures of proteins, i.e. proteomics. Equipment is available for the fractionation of these complex biological mixtures using chromatographic and electrophoretic procedures and for the preparation of protein spots or fractions for identification/analysis. Normally, samples will then be passed on to the appropriate mass spectrometry core facility for that purpose.
Instrumentation housed within this facility includes a PE VICTOR 1420-40 multilabel counter, an infrared imaging system, a benchtop ultracentrifuge, an FPLC system, instrumentation for 2D electrophoresis, ProExpress Imaging System with Progenesis 2D analysis software, a spot-picker for excision of protein spots from gels, MASSPrep for automated proteolytic digestion of proteins and an LC-MALDIPrep that includes a capillary HPLC integrated with a MALDI spotter.
MALDI mass spectrometers are particularly suited for high sample-throughput protein identification of pre-separated or purified samples, such as those obtained from 2-dimensional gel electrophoresis, especially after proteolytic digestion.
The MALDI MS Facility can help you accurately identify and obtain structural information for proteins, peptides and other biopolymers ranging in molecular mass from a few thousand to several hundred thousand Daltons.
Siebens Drake Research Institute, Room G31A Email: firstname.lastname@example.org
The BMSL, a part of the Ontario Wide Protein Identification Facility (OWPIF), features mass spectrometers of several types. These instruments allow the detailed analysis of protein mass and covalent structure through a number of approaches. Some of the works performed at BMSL include: mass determination of polar and/or high molecular weight molecules including peptides, proteins, glycyoproteins, etc.; sequence determination of peptides and peptides from proteins digests; and types and sites of protein modifications.
The BICF houses an array of instrumentation for the biophysical analysis of proteins, peptides and nucleic acids. Clients may use analytical ultracentrifugation, circular dichroism spectropolarimetry, fluorometry, calorimetry, and other techniques to determine molecular weights, secondary structures, stabilities, and to characterize molecular interactions. Most of these techniques require purified samples.
Clients will be provided with expert training, advice and technical assistance in sample preparation and experimentation, in order to discover the properties of their molecules and to achieve their research goals. Expert service work, including interpretation of data as required, is also available.
The Biomolecular NMR Facility houses state-of-the-art nuclear magnetic resonance (NMR) instrumentation and provides expertise required for the characterization of proteins, nucleic acids, carbohydrates and small molecules at the atomic level. A large number of biological NMR experiments and analyses software are available allowing the three-dimensional structure of proteins to be determined in solution, detailed characterization of protein-protein and protein-ligand interactions, and the identification of conformational changes, protein motions (dynamics) and folding processes.
The facility offers training and technical expertise for researchers familiar with NMR techniques, those requiring assistance and first-time users. Researchers may also submit samples for expert data acquisition, analysis and interpretation.
Medical Sciences Building, Room 333 Email: email@example.com
The MCF provides equipment, supplies, and expertise essential for determination of the three-dimensional structures of purified proteins through X-ray crystallography. Equipment includes a crystallization robot, an X-ray generator, and an area detector. Advice and technical assistance in sample preparation and experimentation is provided as needed for clients who wish to conduct the work themselves.
Alternatively, the MCF provides a full crystallization service; clients may submit samples for crystallization trials, and crystallization condition refinement, carried out by the Facility Manager.
How We Can Help You
LRPC facilities are accessible to users from Western University, external academic communities, and industrial settings. Users can perform their own sample analyses or use the services of qualified facility staff.
For further information on how the core facilities of the LRPC can accommodate your research goals, please contact us by email at: