Protein Characterization

Proteins are primarily linear biomacromolecules consisting of amino acids which are connected by peptide bonds. They form secondary and tertiary structures (i.e. several subunits form a functional protein), which can show a high level of complexity with molecular masses of millions of Daltons. Proteins play a pivotal role in many structural and physiological tasks of the cell, some of which are enzymatic catalysis, transport and movement, storage, cellular signalling and immune response – only to name a few.

Both separation and molecular characterization of protein structures are demanding scientific challenges. Wyatt Technology instruments provide the most advanced tools which enable you to successfully design and conduct your studies:

	Absolute molar masses and size/ shape determination of proteins and their aggregates by Multi-Angle Light Scattering (MALS)
	Protein size determination (i.e. hydrodynamic radius) and screening of aggregates by Dynamic Light Scattering (DLS or QELS)
	Separation and fractionation of proteins (without column) by Asymmetic Flow Field-Flow Fractionation (AF4 or FFF)
	Separation by SEC protein columns, specifically designed for SEC-MALS protein applications
	Protein-protein interactions such as reversible self- and hetero-association of proteins, reaction rates and affinities of irreversible aggregation, or virial coefficients by Automated Composition-Gradient Multi-Angle Light Scattering (CG-MALS)
	Absolute Refractive Index (RI) Detection and dn/dc determination at the same wavelength as light scattering detector.

Protein Applications Notes:

#	Description	Download
1	Aggregation of proteins
2	Reverse-phase protein characterization
3	Wheat proteins by reversed phase chromatography
4	Protein modifications using PEGylation to change the drug-delivery properties of a protein.
5	PEGylated protein characterization with the number of PEG attachments!
6	Micro-batch characterization of proteins
7	Aggregation as a function of concentration of proteins.
8	Peptides and proteins showing the power of the miniDAWN for low molar mass characterization of biopolymers.
9	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.
10	Lens proteins--a complex protein which exhibits conformational changes across the molar mass distribution.
11	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.
12	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.
13	How antibodies that are developed to be powerful drugs can bind specifically to a target molecule or cell.
14	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.
15	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.
16	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.
17	To obtain absolute molar masses of heat shock proteins at different temperatures, multi-angle light scattering (MALS) detection was used following SEC.
18	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.
19	Calcium Storage Protein Calsequestrin
20	Hemoglobin Unfolding & Aggregation
21	Refractive index based determination of detergent concentration and its application to the study of membrane proteins
22	Ribosomal Subunits in Protein Biosynthesis
23	Binding Stoichiometry of an Antibody Fragment
24	Kinase Fragment
25	Automated, Online Second Virial Coefficient (A2) Measurements
26	Stoichiometry of Lysin Holoenzyme
27	Low Molecular Weight Lens Peptides and Changes in the Oligomeric Organization of αB-crystallin
28	Molecular weight distribution of gluten proteins analysed by MALS
29	Characterization of Spongiform Encephalopathies
30	Multi-Angle and Dynamic Light Scattering - Role Of Oligomeric Size In Chaperone Function Of αB-Crystallin
31	Soluble Protein-Protein Associations
32	Biophysical Properties of Crystallin Aggregates
33	Novel Malaria Vaccine Candidates
34	Protein Aggregation States
35	Purification of the Rab11-FIP2 Complex

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