| An introduction to differential scanning calorimetry (DSC) | DSC | Various | Microcalorimetry as a tool for structural biology | 
| Antibody characterization in human blood plasma | GCI | Three SARS-CoV-2 antigens and patient plasma samples (diluted to 5%) | Antibody characterization from COVID-19 patient plasma binding to SARS-COV-2 antigens
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| Antibodies - thermal stability | DSC | various monoclonal antibodies | Polyol-induced increases in thermal stability of antibodies by DSC | 
| Antibodies - aggregation | DLS | Monoclonal antibodies | Monoclonal Antibody Characterization | 
| Antibodies - monomer or oligomer (method comparison) | DLS | Immunoglobulin G4 | Comparing Dynamic Light Scattering and the Analytical Ultra Centrifuge | 
| Antibodies - variable domains | DSC | humanized IgG1 anti-bodies, | Contribution of variable domains to the stability of humanized IgG1 monoclonal antibodies | 
| Bacterial toxins - hydrodynamic changes | SEC |  Adenylate cyclase toxin (CyaA) | Characterizing Calcium-induced hydrodynamic changes using SEC with Triple Detection | 
| Bacterial toxins - oligomeric state | SEC | Anthrolysin (ALO) | Overcoming the negative effect of protein structure on molecular weight measurement by Size Exclusion Chromatography – Two protein case studies with Anthrolysin and Bcl-2 | 
| Binding affinity and kinetics – off-rate screening
 | GCI | Eighty-three (83) crude reaction mixtures (CRM) | Rapid optimization of hit and lead compounds 
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| Binding affinity and kinetics – kinetic screening
 | GCI | Collection of small molecules | Molecular interaction analysis by Grating-Coupled interferometry (GCI) 
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| Disaccharides - lower size limits of measurement | DLS | Sucrose | Measuring Sub Nanometer Sizes Using Dynamic Light Scattering | 
| Disaccharides - lower size limits of measurement | DLS | Sucrose | Confirming the Lower Size Specification of the Zetasizer APS | 
| DNA - melting behavior | DSC | Salmon testes DNA (ST- DNA) | Differential Scanning Calorimetry to measure the binding of ions, water and protons in the unfolding of DNA molecules | 
| Enzymes - concentration | DLS | TAKA Amylase | The Measurement of High Concentration Proteins Using DLS: TAKA Amylase | 
| Enzymes - electrophoretic mobility with metal ions | DLS / ELS | Carbonic anhydrase (CA) | Studying the influence of metal ions on the structural stability of carbonic anhydrase with the Zetasizer Nano ZSP: An orthogonal approach | 
| Enzymes - inhibitor mechanisms | DSC | Kinase | Revealing kinase inhibitor mechanisms: ITC leads the way | 
| Enzymes - monomeric vs oligomeric with pH | DLS | Pyrrolidone carboxyl peptidase (PCP) | Oligomeric states of a thermophile | 
| Enzymes - size exclusion | DLS | Bovine Carbonic Anhydrase | Dynamic Light Scattering as a Size Exclusion Chromatography detector | 
| Enzymes - stability with pH | DLS | Lactase | Using Light scattering to study the stability of Lactase | 
| Globular proteins - size and molecular weight | DLS | Myoglobin, Hemoglobin | Size Measurement and Molecular Weight Estimation of Globins using Dynamic Light Scattering | 
| Hormones - contamination, aggregation | DLS | Insulin, amyloids | Minimizing cross-contamination during automated protein analysis | 
| Hormones - contamination, aggregation | DLS | Insulin, amyloids | Ensuring Accurate and Repeatable measurement of proteins using the Zetasizer APS | 
| Hormones – self-association | TDA | Insulin | Assessing the self-association behavior of Insulin with concentration using Taylor Dispersion Analysis | 
| Immunoglobulin - aggregation | SEC | Immunoglobulin G (IgG) | Characterization of IgG monomers and their aggregates | 
| Immunoglobulin - molecular weight, intrinsic velocity | DLS | sRAGE | Measuring conformational changes of sRAGE with intrinsic viscosity | 
| Immunoglobulin - polydispersity | DLS | Immunoglobulin G | Assessing the quality of proteins using light scattering techniques | 
| Immunoglobulin - size distribution | SEC + DLS | Immunoglobulin G4 | Size Exclusion Chromatography Dynamic Light Scattering (SEC-DLS) | 
| Interferons - PEGylation | SEC | Interferon α-5 | PEGylated proteins: Optimizing conjugation reactions using triple detection SEC | 
| Large molecules - aggregation | DLS / SEC | Bovine serum albumin (BSA) | Comparison of SEC-LS and DLS capabilities in the detection and quantification of large protein aggregates | 
| Large molecules - monomers and dimers | DLS + SEC | Human Serum Albumin (HSA), Alcohol dehydrogenase (ADH) | A comparison of the resolution and detection sensitivity of SEC-LS and DLS | 
| Lectins - binding strength | DLS | Concanavalin A | Binding strength of sugars to Concanavalin A | 
| mRNA - riboswitch activity | ITC | Bacterial mRNA | Implementation of kinITC into AFFINImeter | 
| Nanobubbles - size and concentration | NTA | Bovine Serum Albumin and Lysozyme contaminants on surfaces | Nanobubble Applications and Characterization by Nanoparticle Tracking Analysis | 
| Nanoparticles - size and concentration | NTA | Oligonucleotide-functionalized gold colloid | Gold Nanoparticle Applications and Characterization by Nanoparticle Tracking Analysis | 
| Nanoparticles - size and concentration | DLS | Ultrasperical Gold Nanoparticles | Measuring the size of gold nanoparticles using multi-angle dynamic light scattering (MADLS) | 
| Polyglucosides - molecular weight | DLS | Dextran | Characterization of Dextran using Light Scattering Techniques | 
| Polyglucosides - molecular weight | DLS | Dextran | Molecular weight determination of polymers and polysaccharides using the Zetasizer Nano | 
| Polysaccharide polymers - molecular weight and structure | SEC | Chitin/Chitosan | Using triple detection GPC/SEC to determine the molecular weight and structure of Chitosans | 
| Polysaccharide polymers - molecular weight distribution | SEC | Chitin/Chitosan | Characterization of chitosan from various sources | 
| Proteins -  melting behavior | XRD | Thyroglobulin | SAXS study on the thermostability of a protein in solution | 
| Proteins  - molecular weight | SEC | Dextran, Bovine Albumin | Protein and polymer molecular size by GPC/SEC | 
| Proteins - agglomeration | ELS | Lysozyme | Zeta potential measurement of Lysozyme in the High Concentration Zeta Potential Cell | 
| Proteins - aggregate size | DLS | Bovine serum albumin (BSA), β-lactoglobulin, | Combining technologies for the superior detection, separation and characterization of protein aggregates | 
| Proteins - aggregates | DLS | Lysozyme | Adaptive Correlation: Better insight to the presence of aggregates | 
| Proteins - aggregation index | DLS | Immunoglobulin G (IgG) | Enhanced aggregate detection: monitoring protein stability using dual angle light scattering | 
| Proteins - aggregation point | DLS | Ovalbumin | Characterisation of protein aggregation point | 
| Proteins - breakdown to polypeptides | SEC | Alcohol dehydrogenase | Typical protein applications for advanced analytical SEC | 
| Proteins - complexation and binding | DLS | Bovine serum albumin | Characterization of protein-polyelectrolyte complexes | 
| Proteins - crystal structure | XRD | Lysozyme | Transmission diffraction. Measurement and unit cell refinement of lysozyme | 
| Proteins - eliminating cross-contamination | DLS | Bovine serum albumin (BSA) and lysozyme, | Demonstrating that the Zetasizer APS eliminates cross contamination | 
| Proteins - hydrodynamic radius | DLS | Lysozyme | Measurements of 0.1mg/ml Lysozyme in 2μl cell volume | 
| Proteins - hydrodynamic radius, concentration | DLS | Bovine serum albumin | Protein measurements with the Zetasizer µV connected to a GE AKTA SEC system | 
| Proteins - hydrodynamic size and zeta potential | ELS | Human Serum Albumin (HSA) | Improving Protein Zeta Potential Measurements Utilizing A Novel Diffusion Barrier technique | 
| Proteins - ligand binding | NTA | Biotin-Streptavidin complex | Determining fluorescence Limit of Detection with Nanoparticle Tracking Analysis (NTA) | 
| Proteins - microrheology | DLS + ELS | Bovine serum albumin | DLS Microrheology on the Zetasizer Nano ZSP/ZS: Use of a zeta potential pre-measurement step to assess tracer particle-sample interactions | 
| Proteins - modeling concentration effects | DLS | Colloidal silica spheres | Using the Zetasizer Nano to study concentration dependent changes in protein size | 
| Proteins - molecular weight | SEC | Bovine serum albumin | Measuring protein molecular weight using the Viscotek SEC-MALS 20 connected to a Waters Empower® SEC system | 
| Proteins - number and size distribution | DLS | Lysozyme | Number and volume size distributions | 
| Proteins - oligomeric state | SEC | Human serum albumin (HAS) | Characterization of Human Serum Albumin using the Viscotek TDAmax | 
| Proteins - particle size and zeta potential | ELS | Human Serum Albumin (HSA) | Measurements of protein electrophoretic mobility using the Zetasizer Nano ZSP | 
| Proteins - particle size with concentration | DLS | Human Serum Albumin (HSA) | The Effect of Concentration on Dynamic Light Scattering Measurements of Proteins | 
| Proteins - particle size, zeta potential, molecular weight | DLS + ELS | Ferritin | Characterization of Ferritin | 
| Proteins - radius of gyration | XRD | Glucose Imerase | ScatterX78 for BioSAXS studies on dilute protein solutions | 
| Proteins - resolution of mixtures | SEC | Glucose Oxidase, Lactoperoxidase, Lactoferrin, and Lysozyme | Analysis of Protein Mixtures with Multi-Detector SEC | 
| Proteins - size, aggregation with temperature | DLS | Lysozyme and bovine serum albumin (BSA) | Enhanced Protein Aggregation Detection Using Dual Angle Dynamic Light Scattering | 
| Proteins - size titration | DLS + ELS | Bovine serum albumin | Automated protein characterization using the MPT-2 Autotitrator* | 
| Proteins - stability in storage | DLS | Immunoglobulin | Effect of storage conditions on Immunoglobulin | 
| Small molecules: kinetic screening with waveRAPID
 | GCI | Target protein against library of small molecules | Pushing the boundaries in pharmaceutical hit discovery with the novel waveRAPID® kinetic assay  | 
| Small molecules: large target-to-analyte molecular weight
 | GCI | Various small molecule inhibitors of Carbonic Anhydrase II (CAII) | Sensitive kinetic analysis of small molecules binding to large drug targets  |