Purification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary structure of the protein you isolated Please define. Explaining separately what you learned from each experimental finding Show how you came to the conclusion
Purification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary structure of the protein you isolated Please define. Explaining separately what you learned from each experimental finding Show how you came to the conclusion
Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation
Section: Chapter Questions
Problem 17P
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Protein Expression
The method by which living organisms synthesize proteins and further modify and regulate them is called protein expression. Protein expression plays a significant role in several types of research and is highly utilized in molecular biology, biochemistry, and protein research laboratories.
Question
Purification of a new unknown protein that you isolated from tissue and
Assume that you have reached the following data during the characterization;
Gel filtration: Gel filtration in protein native conformation
When chromatographed, it has a molecular weight of 240000 daltons (240
kDa) is detected to be around.
Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride
subjected to gel filtration chromatography again under denatured conditions.
is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa)
a protein is obtained.
SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol
(Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis
being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons.
Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa)
is observed.
In the light of these findings, the quaternary/quaternary structure of the protein you isolated
Please define. Explaining separately what you learned from each experimental finding
Show how you came to the conclusion.
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