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Size-exclusion chromatography, also known as molecular sieve chromatography, [1] is a chromatographic method in which molecules in solution are separated by their shape, and in some cases size. [2] It is usually applied to large molecules or macromolecular complexes such as proteins and industrial polymers . [ 3 ]
Gel permeation chromatography (GPC) [1] is a type of size-exclusion chromatography (SEC), that separates high molecular weight or colloidal analytes on the basis of size or diameter, typically in organic solvents. The technique is often used for the analysis of polymers.
In size exclusion chromatography, where the separation process is driven by entropy, it is not possible to increase the resolution attained by a column via temperature or solvent gradients. Consequently, these separations often require SMB, to extend usable retention time differences between the molecules or particles being separated.
These methods are based on gel filtration chromatography, [2] also called molecular sieve chromatography, which is a form of size-exclusion chromatography. Desalting and buffer exchange are two of the most common gel filtration chromatography applications, and they can be performed using the same resin.
With the advent of size exclusion chromatography (SEC), MALS measurements began to be used in conjunction with an on-line concentration detector to determine absolute molar mass and size of sample fractions eluting from the column, rather than depending on calibration techniques.
Low-angle laser light scattering or LALLS is an application of light scattering that is particularly useful in conjunction with the technique of Size exclusion chromatography, [1] one of the most powerful and widely used techniques to study the molecular mass distribution of a polymer.
Size-exclusion chromatography (SEC) is also known as gel permeation chromatography (GPC) or gel filtration chromatography and separates molecules according to their size (or more accurately according to their hydrodynamic diameter or hydrodynamic volume). Smaller molecules are able to enter the pores of the media and, therefore, molecules are ...
Size-exclusion chromatography separates proteins based on their size. The stationary phase is composed of porous beads that allow smaller molecules to enter the pores while larger molecules pass around them. As a result, larger proteins elute first, followed by smaller ones.
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