Structural Characterization
Protein Profile via One or Two-Dimensional Gel Electrophoresis
| Instrument(s) | Purpose | Photo |
|---|---|---|
| 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 | 
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Molecular Aggregation via Surface Hydrophobicity
| Instrument(s) | Purpose | Photo |
|---|---|---|
| BioTek Synergy HT | To determine protein unfolding and subsequent polymerization driven by hydrophobic interactions To estimate hydrophobic surface area and changes throughout processing | 
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Molecular Aggregation via Surface Charge (Zeta-Potential)
| Instrument(s) | Purpose | Photo |
|---|---|---|
| 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 | 
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Particle size analysis of powders, liquids, and emulsions
| Instrument(s) | Purpose | Photo |
|---|---|---|
| LA-960 HORIBA laser scattering particle size distribution analyzer | To measure particle size of powders, liquids, and oil droplet size in emulsions | 
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Degree of Hydrolysis using OPA method
| Instrument(s) | Purpose | Photo |
|---|---|---|
| Bio-TEK Synergy HT | To determine the degree of hydrolysis and the extent of amine groups blocked by the Maillard reaction | 
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Structural Denaturation using Differential Scanning Calorimetry (DSC)
| Instrument(s) | Purpose | Photo |
|---|---|---|
| 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 | 
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Protein secondary configuration by FTIR
| Instrument(s) | Purpose | Photo |
|---|---|---|
| Fourier-Transform Infrared Spectrometer at the University Characterization Facility | To measure the distribution of secondary protein structures as affected by processing conditions or modification | 
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Protein Tertiary Structures by Surface Enhanced Raman Spectroscopy (SERS)
| Instrument(s) | Purpose | Photo |
|---|---|---|
| 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 | 
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Apparent Protein Aggregation State by Size Exclusion HPLC
| Instrument(s) | Purpose | Photo |
|---|---|---|
| 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 | 
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Chemical Deviation Matrix-Assisted Laser Desorption/Ionization-Time of Flight (MALDI-TOF)
| Instrument(s) | Purpose | Photo |
|---|---|---|
| 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 | 
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Chemical Deviation via LC/MS/MS
| Instrument(s) | Purpose | Photo |
|---|---|---|
| LC/MS/MS available at the University Center for Metabolomics and Proteomics | To separate and identify specific protein subunits | 
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Aggregation via Transmission-Scanning Electron Microscopy (SEM)
| Instrument(s) | Purpose | Photo |
|---|---|---|
| Electron micrscope available at the University Imaging Centers | To visualize protein and particle dynamics (aggregation morphology) | 
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Structural Visualization via Confocal Laser Scanning Microscopy (CLSM)
| Instrument(s) | Purpose | Photo |
|---|---|---|
| Confocal Microscope available at the University Imaging Centers | To visualize protein-protein and protein-lipid interactions in dispersed systems while utilizing fluorescent probes | 
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X-ray Tomography
| Instrument(s) | Purpose | Photo |
|---|---|---|
| X-ray tomography instruments available at the UMN Visible Heart Laboratories | To visualize the morphology of proteins | 
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