9. Lactose exists in two anomeric forms, Draw both anomeric forms of lactose. Why no anomeric forms of sucrose have been reported?
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- 14. What is the difference between a deoxyribonucleotide and a dideoxyribonucleotide? Question 14 options: A dideoxynucleotide is missing a 5'-phosphate group. A deoxynucleotide is missing a 5'-phosphate group. A dideoxynucleotide is missing a 3'- hydroxyl group on its sugar. A deoxynucleotide is missing a 3'-hydroxyl group on its sugar. 15. Which elements are required for DNA to behave as a chromosome in yeast cells: Question 15 options: (can be more than 1) a centromere an autonomous replicating sequence two telomeres Antibiotic selection marker2. 3. Where in your cell can you find the instructions for how to make all of the proteins?*29. In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the structural levels of the protein modified?
- b. What is the difference between the 3' and the 5' ends of a nucleotide chain? C. Do the chains run the same way? d. How are the chains connected? e. Which bases bond to each other? f. What kinds of bonds hold the chain together? 3. What are the main differences between RNA and DNA? 4. Distinguish between the structure of pyrimidines and purines. Explain why adenine bonds only to thymine. 5. Name the five nitrogenous bases in the table below, and put an X in the correct column for each base. Then indicate if the base if found in DNA (D), RNA (R), or both (B) hp6. a.) Which part (sugar, phosphate, or nitrogenous base) of the four types of nucleotides differ? b.) Based on the complementary base pairing rules we know that: A(denosine) pairs with _________ , and that G(uanine) pairs with _________.33. Gel filtration chromatography shows that the molecular weight of a protein is 240,000 Daltons. However, when the protein was subjected to SDS-PAGE in the absence of ß- mercaptoethanol, two polypeptides (100,000 Daltons, 140,000 Daltons) were identified. Furthermore, when the protein was subjected to SDS-PAGE in the presence of ß- mercaptoethanol, three polypeptides (100,000 Daltons, 90,000 Daltons, and 50,000 Daltons) were identified. Which of the following statements is true of the protein? A. The protein is composed of three polypeptides. B. The three-dimensional structure of the protein is stabilized by both covalent and non- covalent bonds. C. Both A and B. D. Neither A nor B. 34. What is purpose of SDS in SDS-PAGE? E. To selectively bind the target protein F. To maintain buffer pH in the gel G. To cause the separation of proteins to be on the basis of molecular weight only H. To initiate polymerization of acrylamide to form gel
- A. Consider the dipeptideVal–Pro: What amino acid is the N terminal aminoacid? What amino acid is the C terminal aminoacid? How are the amino acids connected? Give the name of the dipeptide. Give the name of the dipeptide in which the amino acid order is reversed as Pro–Val.13. a. Draw in the corresponding DNA nucleotide that would base pair with the adenine nucleotide shown below using the same level of detail as provided in the image below. Hint: Remember that DNA bases pair in the antiparallel orientation. орасна you A OH H b. How do you know the adenine nucleotide drawn above is from DNA and not RNA?4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…
- 20. Nucleosides consist of a nitrogenous base bound by an N-glycosyl linkage to a phosphorylated pentose. true or falseYour friend has discovered a protein that they suspect is glycosylated. They decide to perform a series of tests to determine the nature of the oligosaccharide. Assuming/Knowing the following: Fucose molecular weight is approximately 164 Galactose molecular weight is approximately 180 GalNAc molecular weight is approximately 221 Mannose molecular weight is approximately 180 Sialic Acid molecular weight is approximately 309 Neuraminidase cleaves before a Sialic Acid (Sialic Acid and anything after leaves the protein) Beta-galactosidase cleaves after a Galactose (Galactose and anything before remains on the protein) Peanut Agglutinin binds to GalNAc Concanavalin A binds to Mannose Hemagglutinin binds to Sialic Acid Based on preliminary results, they suspect that the oligosaccharide is 7 glycosides long and weighs a total of 1414 g/mol They carried out the following experiments: they treated the protein with either a glycosidase or a lectin, and then pelleted the protein using…1 Draw the following polypeptide: Met- Tyr-Val-Ser-Asn 2A Draw the hydrolysis of a dipeptide consisting of phenylaline and glutamic acid. 2B What are the fuctional group present in the side chains of the amino acids.( phenylalanine and glutamic acid) 2C are the sidechains in part 2B hydrophobic or polar 2D where would you expect to find them ( surface or interior of a protein) ? why ?
