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Sub-Part Questions:

What information about a protein can be obtained by SDS-PAGE?

What is the role of detergent (SDS) in SDS-PAGE?

What is the role of the polyacrylamide gel?

How do you determine the size of a protein based on the results of SDS-PAGE?

What was Maud Menton’s contribution to the development of the technique?

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Deanna Hettinger
Deanna HettingerLv2
29 Sep 2019

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Related questions

A student given the task of purifying a protein found that the protein had a molecular mass of 400kDa when measured by gel filtration chromatography. (This technique involves the use of a column packed with material that functions like a molecular sieve. No harsh reagents are used so it preserves the native structure of the protein. ). The student wanted to confirm the purity of the protein by SDS-PAGE. When the protein was analyzed by polyacrylamide gel electrophoresis in the presence of SDS, 3 bands with the following molecular weights were obtained: 180, 160, 60kDa. However, the student realized that he/she forgot to add 2-mercaptoethanol to the sample gel buffer when it was made up. So the student ran the gel again, this time in the presence of SDS and 2-mercaptoethanol. This time, 3 bands were observed as before, however, the molecular weights were 160, 90, and 60kDa. If you were that student what would you conclude about this set of observations?

What would be the advantage of using two independent techniques (gel filtration and SDS-PAGE) to characterize a protein?

ou are studying a protein that you think consists of a heterodimer composed of a 30 kDa and a 40 kDa subunit, which are joined together by disulphide bonds. In addition to your protein sample you have available a SDS-PAGE gel, an electrophesis apparatus like the one you used in the laboratory, and a Bio-Rad Precision Protein Kaleidoscope standard (Bio-Rad catalogue number 161-0375). You also have access to two different sample buffers. Buffer A contains 4% (v/v) SDS and 5% (v/v) ß-mercapto ethanol. Buffer B contains 4% (v/v) SDS but no ß-mercapto ethanol. As per the practical, samples are heated at 95oC for 4 minues before they are loaded onto an SDS-PAGE gel and electrophoresed.

3a) Describe the experimental methods that would allow you to test your hypothesis. Provide sufficient detail such that an interested reader could faithfully repeat your experiment. In your answer describe the chemistry and biochemistry involved in your treatment. Must be less than 200 words HYPOTHESIS IS : ABOUT IF IT IS A GERODIMER AND COMPOSED OF DISULPHDIDE BONDS NOTE THERE IS NO DYE PRESENT SO HOW CAN I SEE THE RESULTS OF ELECTROPHORESIS WITHOUT? AND WITH THE MATERIALS LISTED ABOVE

1. Introductory sentence explaining the topic area

2. Main aim and hypothesis being tested

3. General methods used

4. Results obtained

5. Conclusion

Provide a short written comment that describes the strengths and weaknesses IN THIS PARAGRAPH.

The study of Osteogenesis Imperfecta and what causes it is important and the diagnosis of it is very important especially to those who may be affected by the illness. The diagnosis is what we are focusing on, the illness is caused by most commonly caused by the mutation in the collagen genes, specifically α1 collagen. This leads us to try to find this illness in a young boy, called Alexander Brown. We are trying to find out if this young boy has the illness commonly known as brittle bone disease, and we do this by extracting the collagen from normal un-affected cells and Alexanders cells, purifying the collagen and then running it through a Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) to separate out the various sizes of proteins left in the collagen. After running this SDS-PAGE we were able to compare the unaffected patterns of size to the cells collected from Alexander Brown however there can be no firm conclusions drawn from these results, the image taken of the SDS PAGE was blurred and pixelated as well as being very blue.

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