The BCMB department has access to a large collection of instrumentation for biophysical and biochemical characterization of proteins and nucleic acids under the heading of the Bioanalytical Resources Facility (BRF). This facility provides training to all students and researchers in the department. Additionally, teaching modules are available for most instruments. Also, the facility performs all routine maintenance and calibrations for the instruments, solves minor instrument issues and serves as the contact person for service engineers for major instrument problems.
The instruments available include:
Analytical Ultracentrifuge (AUC) A Beckman XL-I is utilized in the department to study proteins, peptides and nucleic acids. This technique is used to determine sedimentation coefficient, molar mass, purity and oligomeric state of a sample, as well as the stoichiometry and affinity of interactions.
Circular Dichroism (CD) An Aviv 202 CD spectrophotometer is used by researchers in the department to determine whether a protein is folded, characterize the global secondary structure of a protein and monitor folding and unfolding as a function of temperature, pH or denaturant concentration.
Differential Scanning Calorimeter (DSC) A VP-DSC is available to measure protein stability and energetics of unfolding and folding.
Electron Paramagnetic Resonance (EPR) Bruker EMX (X-band) Spectrometer is used to identify paramagnetic metals in a sample, quantify metal binding to a protein, study conformational changes and protein dynamics and monitor changes in the redox state of a system.
Fluorescence Spectroscopy A Perkin Elmer LS 55 used by researchers to monitor protein folding, conformational changes, dynamics and binding interactions.
High Performance Liquid Chromatography (HPLC) An Agilent 1200 system is used in the department for separation of proteins, peptides and small molecules. This instrument is often used to prepare samples for mass spectrometry.
Isothermal Titration Calorimeters (ITC) Two VP-ITC instruments are used to measure affinity and thermodynamic parameters of interactions. Experiments evaluating protein-protein, protein-small molecule, protein-nucleic acid and protein-metal complexes are currently being performed in the department.
Mass Spectrometry A Bruker MALDI-TOF Mass Spectrometer is used in the department for accurate mass measurements of proteins and peptides
Surface Plasmon Resonance Spectrometer (SPR) A Biacore 3000 is used in the department to study biomolecular interactions. This technique not only measures binding affinity, but also quantifies the kinetics of the interaction. Binding events involving proteins, nucleic acids, carbohydrates and other small molecules are amenable to SPR analysis.
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