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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.

Molecular dynamics and “reactions”: quantifying motional properties and possible to look at timescales between ps and days

Assess stability and folding of proteins

Elucidation of structure of biomarkers, metabolites, and synthetic pathways

Metabolomics for bio-fluids and tissues

Thermal analysis which can be coupled with GC-MS for the determination of:

Melting point using either Differential Thermal Analysis or Differential Scanning Calorimetry

Crystallization transition using either Differential Thermal Analysis or Differential Scanning Calorimetry

Glass transition using Differential Scanning Calorimetry

Decomposition temperature using ThermoGravimetric analysis which can be coupled with GC-MS for the identification of the decomposition products

Temperature of combustion with ThermoGravimetric analysis and identification of combustion volatiles using GC-MS

Qualitative and Quantitative elemental analyses

Halide determination (Chlorine, Bromine, Iodine) in solids or liquids using X-ray Fluorescence Spectroscopy

Survey of impurities and elements heavier than Sodium with X-ray Fluorescence Spectroscopy

Optical spectroscopy

Determination of functional groups and likely solvent molecules using Infrared (IR) spectroscopy

Vibrational stretches using Raman and IR Spesctroscopy

Color, band gap, and absorption measurements using Ultra-violet (UV), visible (Vis), and IR spectroscopies

Photoluminescence, lifetime phosphorescence, and emission measurements using spectrofluorimeter

Optical rotations and quantification of enantiomers using polarimetry