Protein Characterization

Molecular Characterization of proteins and protein structures are demanding scientific challenges. Wyatt Technology instruments provide the most advanced tools which enable you to successfully design and conduct your studies:

Typical Applications:

Proteins analytics:

  • Absolute molar mass determination using MALS (SLS)
  • Identification of proteins by their molar mass
  • Identification of the proteins oligomeric state (monomer, dimer, etc.)
  • Identification and characterization (mass, size and shape) of aggregates
  • Size measurement coupled to chromatography and in batch mode
  • Identification of folded / unfolded proteins
  • Identification of conformational changes
  • Characterization of the solubility of proteins
  • Determination of protein-protein interactions
  • Investigation of peak purity for protein purification
  • Separation and characterization of viruses and vaccines
  • Determination of the viscosity of protein solutions
  • Separation of proteins using SEC and FFF
  • Semi-preparative protein purification

Modified proteins:

  • Molar mass, size and stoichiometry of protein-protein complexes
  • Molar mass of the different components of the complex
  • Molar mass, size and stoichiometry of pegylated and glycosylated proteins
  • Molar mass of modifier and protein
  • Molar mass of membrane protein
  • Size and mass of micelle and membrane protein
  • Analyse der Quartärstruktur eines Membranproteins

Protein Formulation

  • High-throughput screening of formulations
  • Determination of protein stability and thermal stability

Protein Crystallization

  • Evaluation if protein is supposed to crystallize
  • Determination of protein stability, thermal stability
  • Screening for crystallization conditions 

Protein Application Notes:

# Description Download

Characterization of a Monoclonal Antibody with Wyatt Technology’s MALS and RI detectors and a bio-inert HPLC

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Rapid, Autonomous Lot-to-Lot Comparability of Monoclonal Antibodies with the Calypso

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Characterization of Heparin Binding to Tau Protein via CG-MALS

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Monoclonal Antibodies and the Preparative Use of Flow Field-Flow Fractionation (AF4)

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Aggregation of proteins

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Reverse-phase protein characterization

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Wheat proteins by reversed phase chromatography

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Protein modifications using PEGylation to change the drug-delivery properties of a protein.

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PEGylated protein characterization with the number of PEG attachments!

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Micro-batch characterization of proteins

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Aggregation as a function of concentration of proteins.

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Peptides and proteins showing the power of the miniDAWN for low molar mass characterization of biopolymers.

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Hemoglobin--One of the building blocks of life! This note examines the elution properties of this protein and how different they are from more "conventional" proteins.

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Lens proteins--a complex protein which exhibits conformational changes across the molar mass distribution.

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Gelatins--Used in everything from food thickening agents to photographic film substrates, gelatins can be analyzed successfully and absolutely with SEC-MALS, as this note shows.

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Protein-Protein Interactions--Scientists working at Pfizer's Central Research Laboratory show that the DAWN is an invaluable tool for the development of a scale-up purification protocol.

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How antibodies that are developed to be powerful drugs can bind specifically to a target molecule or cell.

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This note concerns the use of an infrared (IR) laser in characterizing a protein that fluoresces at the red wavelength, but did not fluoresce at the longer IR wavelength.

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It discusses the application of MALS-QELS interfacing to enable absolute molar mass and size determinations from 1nm to 500nm. In this note we use BSA, as well as a glycoprotein sample to show the range of masses and sizes we can characterize by both static and dynamic light scattering.

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Proteins can elute at radically different times depending on their structure, yet simple column chromatography misses this completely. By adding a MALS with the WyattQELS accessory, the subtleties of proteins may be studied.

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To obtain absolute molar masses of heat shock proteins at different temperatures, multi-angle light scattering (MALS) detection was used following SEC.

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Membrane protein is generally soluble only in the presence of micelles; thus, it is very difficult to characterize the oligomerization state of the membrane protein in a lipid-containing solvent. In this application note we demonstrate the use of multi-angle light scattering (MALS) detection in combination with UV absorption and differential refractive index (DRI) detection to determine the molar masses (MM) of both the core protein and the entire protein-lipid complex.

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Calcium Storage Protein Calsequestrin

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Hemoglobin Unfolding & Aggregation

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Refractive index based determination of detergent concentration and its application to the study of membrane proteins

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Ribosomal Subunits in Protein Biosynthesis

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Binding Stoichiometry of an Antibody Fragment

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Kinase Fragment

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Automated, Online Second Virial Coefficient (A2) Measurements

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Stoichiometry of Lysin Holoenzyme

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Low Molecular Weight Lens Peptides and Changes in the Oligomeric Organization of αB-crystallin

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Molecular weight distribution of gluten proteins analysed by MALS

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Characterization of Spongiform Encephalopathies

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Multi-Angle and Dynamic Light Scattering - Role Of Oligomeric Size In Chaperone Function Of αB-Crystallin

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Soluble Protein-Protein Associations

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Biophysical Properties of Crystallin Aggregates

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Novel Malaria Vaccine Candidates

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Protein Aggregation States

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Purification of the Rab11-FIP2 Complex

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Do you want more information? We would be delighted to hear from you!