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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

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

Accurate determination of concentration of Carbon, Hydrogen, Nitrogen, and Sulfur in solid materials by using combustion CHNS analysis

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