In kappa and iota carrageenans, gels are formed through double helical formation of two polysaccharide segments via covalent interactions. True False
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In kappa and iota carrageenans, gels are formed through double helical formation of two polysaccharide segments via covalent interactions.
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- Discuss three polysaccharide structural features that promote gel formationOn 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%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 bonds
- 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.SDS-PAGE gels separate proteins by charge. Therefore proteins that are 10,000 daltons (g/mol) will move the same distance as proteins that are 80,000 daltons (g/mol). This statement is: True or False (And why)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.
- a protein pretreated with an sds page detergent shows two bands around 100 and 150 kD on the electrophoresis gel.Same protein is treated with the SDS and 2-mercaptoethanol reveal a single band 50 kd on gel.How many subunits would this protein containA mixture containing aspartic, lysine, serine and tyrosine was subjected to gel electrophoresis at pH 7.0. Indicate the position of each amino acid in the gel. (Show comprehensive explanation, and with graphical illustration if possible).After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?
- You analyze a protein of 100 kDa using SDS-PAGE in the absence and presence of �-mercaptoethanol (BME) and observe the following band pattern in the gels: Which of the following statements about the protein is correct? (the image is attached) a. The protein consists of three polypeptide chains, two of which are connected via S-S bridges. b. The protein consists of two different polypeptide chains connected via S-S bridges. c. The protein has two different folding conformations. d. The protein consists of two different polypeptide chains linked to each other via non-covalent interactions.does all 20 amino acids soluble in organic solvents like acetone and chloroform? true or falseDescribe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.