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- Each of the ff. involves a disorder in the function of an organelle or other cell structure. Identify the cell organelle or cell structure involved and indicate whether it is likely to be underactive or active. a) A baby is placed on a low phenylalanine diet as his newborn screening results revealed that he inherited phenylketonuria. b) A girl suddenly felt weak and manifested cyanide poisoning symptoms after ingesting undercooked cassava which contains cyanoglycosides. c) A man develops pleiomorphic liposarcoma (rare cancer). The cause of the problem is a hard mass of cells in his right inner thigh that rapidly increased in size in a matter of 2 months. d) A male chef learns that he is infertile because his sperm are non-motile. Helping tags: biology, cell biology, cell structure, cell organelleName an example of each of the following classes ofcompounds:a. glycoproteinb. proteoglycanc. disaccharided. glycosaminoglycan (GAG)Which of the following statements regarding adenosine phosphates is incorrect? a) ATP, ADP and AMP are all examples of adenosine phosphates. b) All adenosine phosphates contain a pentose ribose sugar. c) All phosphate ions in adenosine phosphates are joint together by a phosphoanhydride bond. d) All adenosine phosphates releases energy upon cleavage of phosphate group.
- In animal cells, enzymes synthesized to hydrolyze polymers to form monomers. This process involves the RER, the SER and the Golgi apparatus. In which of the following is the molecule listed for this process employed by the cells of the organ indicated? a) formation of Fatty acids by lipases in the small intestine. b) production of glucose from glycogen by the liver. c) formation of amino acids by proteases in the small intestine d) formation of monosaccharides by Carboxylases in the mouth and small intestine. e) all are possibleProtein structure and function: a) Name two common post-translational modifications of proteins in the cell that will affect their structure/function. b) What are prions? Briefly describe their structure and function. C) Explain the principles of protein folding and significance of urea and Bmercaptoethanol in the experimental procedures addressing this question.Deduce the amino acid sequence of a polypeptide from the following:1. Acid hydrolysis gives Ala2, Arg, Lys2, Met, Phe, Ser22. Carboxypeptidase gives Ala3. Trypsin digestion gives 4 peptides a) Ala, Arg b) Lys, Phe, Ser c) Lys d) Ala, Met, Ser4. CNBr treatment gives a) Ala, Arg, Lys2, homoserine, Phe, Ser b) Ala, Ser5. Thermolysin is a protease that cuts on the N-terminal side of hydrophobic amino acids (substrate preference is Leu, Ile, Phe, Trp, Tyr, Val). Thermolysin treatment of our polypeptide yields 2 peptides a) Ala, Arg, Ser b) Ala, Lys2, Met, Phe, Ser
- Define the following terms:a. proproteinb. preproproteinc. disulfide exchanged. proline hydroxylatione. proteolytic cleavageO-linked glycosylation occurs on ___ residues of proteins. a) Serine and Threonine b) Asparagine c) Methionine d) Acidic amino acid residuesDefine the following terms: a. GPI anchor b. glycolipid c. glycoprotein d. glycoconjugate e. proteoglycan
- Protein kinases (PTKS) are enzymes that regulate the biological activity of proteins by phosphorylation of specific amino acids, inducing a conformational change from an inactive to an active form of the protein. a) True b) FalseImagine that a mutation has been discovered in the HBA1 gene, where amino acid residue # 1 in the alpha subunit is changed from valine to lysine. The structure of these two amino acids is shown below. How would this mutation affect the mobility of HbA in the gel?a) HbA with this mutation would have the same mobility as normal HbAb) HbA with this mutation would have the same mobility as HbSc) HbA with this mutation would have a faster mobility than normal HbA O d) HbA with this mutation would have a mobility somewhere in between HbS and normal HbAThe alkaline hydrolysis of pAUGCAGC oligonucleotide produces: O A. Uridine 2'-monophosphate, uridine 3'-monophosphate, cytosine 2'-monophosphate O B. Adenosine 2'-monophosphate, adenosine 3'-monophosphate, adenosine 21,5'-bisphosphate OC. Guanosine 2'-monophosphate, guanosine 3'-monophosphate, cytosine 3'-monophosphate O D. Cytidine 3'-monophosphate, guanosine 2'-monophosphate, adenine 2'-monophosphate O E. Adenine 3,5'-bisphosphate, guanine 2,5'-bisphosphate, uridine 2'-monophosphate O F. Uridine 2'-monophosphate, uridine 3'-monophosphate, guanine 3'-monophosphate