Purchase Solution

size exclusion chromatography and SDS-PAGE

Not what you're looking for?

Ask Custom Question

Describe whether, and how, size exclusion chromatography and SDS-PAGE can be used to determine the molecular weight and oligomeric status of a protein. Indicate whether it is necessary to compare the protein's mobility relative to standards of known molecular weight.

Purchase this Solution
Solution Summary

This solution describes how size exclusion chromatography and SDS-PAGE can be used to determine the molecular weight and oligomeric status of a protein.

Solution Preview

In size-exclusion chromatography, molecules are separated according their physical size, not by molecular weight. however; the molecular weight can be calculated by relating the hydrodynamic volume (space taken up by the molecule in solution) to the hydrodynamic volume of polystyrene, which must be used as a standard with this technique. As the relationship between ...

Purchase this Solution
Free BrainMass Quizzes
General Chemistry - Classification of Matter

This test will assess your knowledge on the classification of matter which includes elements, compounds and mixtures.

Match Elements with their Symbols

Elements are provided: choose the matching one- or two-letter symbol for each element.

Thermochemistry

The quiz helps in revising basic concepts about thermochemistry.

Functional groups in Organic Chemistry

You will be tested on the names of functional groups in Organic Chemistry. It is very important to know the functional groups to understand Organic reactions.

Organic Chemistry Naming: Alkanes

This is a quiz which is designed to assist students with learning the nomenclature used to identify organic compounds. This quiz focuses on the organic compounds called Alkanes.

View More Free Quizzes
Related BrainMass Solutions

  • Protein Purity

    Since the charges of all proteins are fairly equal, this method separates them almost entirely based on size. SDS-PAGE is often used to test the purity of a protein after each step in a series.

  • Protein Purification Questions

    Finally, SDS-PAGE is done to further separate GOT from other proteins in the sample. Separation via SDS-PAGE is through differences in molecular size.

  • five step protocol

    However, when you run the purified enzyme on a SDS-PAGE gel, you obtain two different sized peptides one 30 kD and the other 20 kD. What could be the possible explanations for this result?

  • Why scientists purify proteins; principle of size exclusion

    How does size exclusion chromatography works? Size exclusion chromatography or gel filtration chromatography works on the principle of separation of proteins on the basis of their size. The column is packed with a matrix of fine porous beads.

  • Gel-Filtration / Size Exclusion Chromatography

    size exclusion chromatography is examined.

  • Analyzing Western Blots, etc.

    It also serves a very important purpose besides telling about size of the proteins. Imagine protein purification did not work and you did not add protein markers to your SDS-PAGE.

  • Interpreting SDS-PAGE Gels

    Background about SDS-PAGE Polyacrylamide gel electrophoresis (PAGE) is a simple technique for separating bio-macromolecules such as proteins and DNA on the basis of size (ie molecular weight).

  • Considering Protein Structure

    B) SDS-PAGE separates proteins on the basis of size under reducing and denaturing conditions. So if our protein is comprised of more than one subunit, and if those subunits are of different sizes, then they will appear as distinct bands on the gel.

  • 4 Analytical Chemistry Questions.

    4. molecular exclusion chromatography 5. affinity chromatography a.

View More Related Solutions