Capabilities - Structural Characterization

Densitometer to scan gels and determine protein band densities (BioRad)

To determine the protein profile under reducing and non-reducing conditions

To reveal polymerization and/or hydrolysis patterns, potential bonding mechanisms, and the prevalence of individual protein subunits

BioTek Synergy HT

To determine protein unfolding and subsequent polymerization driven by hydrophobic interactions

To estimate hydrophobic surface area and changes throughout processing

Malvern Zetasizer zeta potential and particle size analysis

To estimate the net charge density on the surface

To indicate any changes in surface hydrophilicity, protein unfolding, and possible interactions with macromolecules such as carbohydrates

LA-960 HORIBA laser scattering particle size distribution analyzer

To measure particle size of powders, liquids, and oil droplet size in emulsions

Bio-TEK Synergy HT

To determine the degree of hydrolysis and the extent of amine groups blocked by the Maillard reaction

Mettler Toledo DSC1 differential scanning calorimetry

To determine the onset temperature of denaturation and the degree of unfolding as affected by processing or modification

To estimate protein denaturation state

Fourier-Transform Infrared Spectrometer at the University Characterization Facility

To measure the distribution of secondary protein structures as affected by processing conditions or modification

HORIBA LabRAM Odyssey Confocal Raman Microscope using Surface Enhanced Raman Spectroscopy (SERS) available at the University Characterization Facility

To determine the distribution of tertiary protein structures and intramolecular interactions as affected by processing conditions or modification

Shimadzu LC-2050C 3D*

To identify degree of polymerization, the extent of intermolecular aggregation with covalent and non-covalent linkages, and molecular weight of polymer distribution

MALDI_TOF available at the University Center for Metabolomics and Proteomics

To determine the individual protein subunit/peptide molecular weights, which can be used for identification of different protein subunits

To identify changes in proteins and peptides profile/distribution as affected by processing and/or enzyme modification

To monitor the site of modification

LC/MS/MS available at the University Center for Metabolomics and Proteomics

To separate and identify specific protein subunits

Electron micrscope available at the University Imaging Centers

To visualize protein and particle dynamics (aggregation morphology)

Confocal Microscope available at the University Imaging Centers

To visualize protein-protein and protein-lipid interactions in dispersed systems while utilizing fluorescent probes

X-ray tomography instruments available at the UMN Visible Heart Laboratories

To visualize the morphology of proteins