Applications for Bioanalytical
IMSERC has a large pool of modern instrumentation for bioanalytical scientists. Our center is integrated with the Chemistry Department at Northwestern University where scientists run their experiments on a 24/7 basis. From monitoring reactions to full structure elucidation, researchers and students have access to a variety of techniques that can be used for:
Crystallographic atomic structure determination, identification, and refinement of organic and inorganic compounds for extraction of structural information such as:
Determination of unit cell and bonding environment (bond-lengths, bond-angles, cation-anion coordination, site-ordering, etc.)
Determination of packing of molecules and co-crystals
Determination of Hydrogen bonding
Determination of enantiomers
Refinement of co-crystals, modulated, and twinned structures (incommensurate, commensurate, composite superstructures)
High resolution data for charge density measurement and precise assignment of atoms with similar chemical environment
Powder evaluation of sample purity (sensitivity of ~2% by weight)
Quantitative determination of individual crystalline phases and impurities in mixtures of powder
Monitor reactions in real time as a function of time, temperature, pressure, and gas flow/pressure
Probe catalytic changes to substrates
Investigate decomposition mechanism
In-situ monitoring of crystallization processes with increasing temperature
Mass Spectrometry
Untargeted Lipidomics Profiling
Lipids play an important role in the cell, tissue, and organ physiology, not only acting as structural components of cell membranes, but also imporant signaling molecules and vital substrates to various protein complexes. Untargeted lipidomics analyses enable a comprehensive survey of the lipidome composition between different samples
Mass Spectrometry Imaging (MSI) of Tissues and Cell Cultures
MS Imaging is a label-free method to obtain spatial distribution and abundance of lipids, drugs, drug metabolites, proteins, peptides and glycans in tissue sections or directaly from cell culture grown in poly-lysine-coated ITO slides.
Intact Mass Determination of Proteins
Post-translation modification or the addition of ligands to specific sites can be verified using our high-resolution mass spectrometers. Native-like conditions is possible upon request using an SEC column and ammonium acetate mobile phase.
Metabolite profiling by LC-MS/MS
Using our high-resolution mass spectrometer, coupled to an UHPLC capable using various chromatography methods, we can profile the metabolome of various biological extracts by identifying at the MS1 or MS2 (MS/MS) level.
Absolute quantification of biomolecules and drug therapeutics in tissue, serum, plasma, and urine
Absolute quantification of endogenous biomocules or drug therapeutics can be accomplished using our higly senstitive instruments.
Nuclear Magnetic Resonance
Structural Biology with NMR
With modern digital NMR equipment, rapid protein structure determination with solution NMR is a reality for proteins with molecular weight below 25 kDa. It is straight forward to get a three-dimensional solution NMR structure or a protein or protein ligand complex in its native functional state. In addition to providing insights about their three-dimensional structures and functions, it can also be employed to probe the protein or enzyme active sites and folding changes associated with enzyme activation.
Molecular interactions/Binding studies (Proteins, DNA, Ligands)
NMR is a powerful technique to study macromolecule (protein, DNA, and RNA) ligand binding.