SDS-PAGE gels are useful in determining the molecular weights of proteins; however, the molecular weights of are usually not reliable. protei
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- Why do we use a stacking gel in SDS-PAGEHow stacking and resolving gels are prepared in SDS-PAGE? Discuss the role of each ingredient used in preparing SDS-PAGE.Gradient PAGE uses differing gel concentrations along the length of the gel to achieve optimalseparation of proteins of a wide range of molecular weight proteins. How does the staining pattern of these types of gels differ from nongradient PAGE?
- What types of macromolecules are usually separated on agarose electrophoresis gels?Define about sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE)? Explain importance of sodiumdodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) ?In kappa and iota carrageenans, gels are formed through double helical formation of two polysaccharide segments via covalent interactions. True False
- What is the function of sodium dodecyl sulfate (SDS) in SDS-PAGE? stabilizes the gel matrix, improving resolution during electrophoresis SDS solubilizes proteins to give them uniformly negative charges, so the separation is based purely on size. SDS raises the pH of the gel, separating multiunit proteins into individual subunits. SDS solubilizes proteins to give them uniformly positive charges, so separation is based purely on pH.topic: sds-page gel What is the purpose of adding APS and TEMEDHigh salt concentrations tend to cause protein aggregation. Suggest a way to identify proteins normalexpressed in particular bacterial species that can retaintheir solubility despite high salt conditions.
- Given the description of four different proteins above: Which protein will have the highest mobility in an SDS-PAGE gel?How many copies of a protein need to be presentin a cell in order for it to be visible as a band on an SDSgel? Assume that you can load 100 μg of cell extract ontoa gel and that you can detect 10 ng in a single band by sil-ver staining the gel. The concentration of protein in cellsis about 200 mg/mL, and a typical mammalian cell has avolume of about 1000 μm3 and a typical bacterium a vol-ume of about 1 μm3. Given these parameters, calculatethe number of copies of a 120-kd protein that would needto be present in a mammalian cell and in a bacterium inorder to give a detectable band on a gel. You might try anorder-of-magnitude guess before you make the calcula-tions.a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain