Discuss three polysaccharide structural features that promote gel formation
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Discuss three polysaccharide structural features that promote gel formation
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- Discuss three polysaccharide structural features that promote gel formation. Include a polysaccharide example for each feature in your discussion.On an SDS-gel, If the distance traveled by the bromophenol blue dye is 7 cm, and the distance traveled by the protein band is 2.1 cm, the mobility of the protein is 0.3 30 3 30%Sketch the appearance after visualization of a protein mixture containing the seven proteins above when subjected to two-dimensional (2D) gel electrophoresis.
- Describe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bondsOf the components in the hydrogels beads, which is the protein we are interested in measuring?
- The given protein, Protein X, is a heterotrimer - meaning it is a multimeric protein consisting of different polypeptide chains. Its molecular weight is 200 kDa. Using SDS-PAGE, the protein was characterized and the following profile is the result (attached in the picture). 1: Standard Protein Ladder 2: Protein X solution 3: Protein X solution + β-mercaptoethanol Based on the given gel profile in the picture, can it be concluded that the solution of Protein X is pure? Explain. can it be concluded that disulfide bonds hold together Protein X's quaternary structure? Explain.Describe the chemistry involved in the processes of Lipid Interesterification and Lipid Fractionation. How can these two processes be combined to provide a spreadable lipid from palm oil? (Please provide a detailed explanation).Define the term pI, describe its meaning and how it could be used to separate proteins using a 2D isoelectric focusing gel.
- Sketch the appearance after visualization of a protein mixture containing the seven proteins (fibrinogen, y-globulin, collagen, ovalbumin, myoglobin, hemoglobin, insulin) when subjected to two-dimensional (2D) gel electrophoresis.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?As an example, consider albumin, a protein made of a single polypeptide weighing 66,000 daltons (66 kDa). On the other hand, gamma globulin has quaternary structure: is made of four polypeptides, two of which weigh 23,000 daltons (23 kDa) each, and two of which weigh 53,000 daltons (53 kDa) each. When treated with reducing agent and SDS, the subunits separate and they all linearize. If albumin and gamma globulin were run through gel electrophoresis, which polypeptides would move the fastest? Which would move the slowest?