1. What is the role of plant glycobiology in facilitating nitrogen fixation? 2. N-linked glycosylation in plants shares many similarities with N-linked glycosylation in mammalian cells. Describe at least two structural features that are shared between plant and mammalian N-linked glycans. Similarly, describe at least two structural features that are different.
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1. What is the role of plant glycobiology in facilitating nitrogen fixation?
2. N-linked glycosylation in plants shares many similarities with N-linked glycosylation in mammalian cells. Describe at least two structural features that are shared between plant and mammalian N-linked glycans. Similarly, describe at least two structural features that are different.
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- 1. What is the pathway involved during the lipid utilization into glucose in plants? 2. What is the glycolytic substrate responsible for the entry of Mannose in the preparatory stage of glycolysis?1. What is the distinguishing structural feature of O-glycans? 2. What other prominent class of glycoproteins besides mucins is known for the presence of O-linked glycans?1.Linoleic acid and linoleic acid cannot be synthesized in human tissues, because of _____. * a.Human cells cannot synthesize unsaturated fatty acids. b.Human cells can synthesize only mono-unsaturated fatty acids. c.The corresponding biosynthetic pathway was lost during evolution. d.Humans are diploid organisms; only polyploidy organisms have enough genes for the synthesis of these fatty acids 2.What product could be formed from the breakdown of amylopectin and cellulose? * a.Cellulose could be broken down into chitin b.Cellulose could be broken down into sucrose c.Amylopectin could be broken down into maltose d.Amylopectin could be broken down into glucosamine 3. Which characteristics distinguishes amylopectin and glycogen? * a.Only glycogen has a coiled shape. b.They have different degrees of branching c.Only amylopectin can form hydrogen bonds d.They have different types of glycosidic bond
- 1. How is creatine biochemically formed in mammalian cells? 2. Why would it be more correct to call concentrated ammonium hydroxide by the alternative name ammonia water?1. If a molecule is interating with its side chains of an enzymes active site but it is not the substrate of the enzyme what kind of enzyme regulation is this? 2. What is the change in thetype of bond between Ser 80 -> Arg. 3. Will this change cause the complex to be more or less stable. Explain1. Which of the following pathways of information flow has never been observed on Earth? chose all that apply a. From RNA to DNA b. From RNA to Protein c. From DNA to RNA d. From Protein to RNA e. From Protein to DNA f. From DNA to Protein 2. Which biosynthetic pathways are downregulated by the products of the de novo purine biosynthesis pathway? Choose all that apply a. The de novo pyrimidine biosynthesis pathway b. The pyrimidine salvage pathway c. The pathway to 5-phosphoribose-1-pyrophosphate (PRPP) d. The de novo purine biosynthesis pathway e. The pathway to the amino acid histidine f. The purine salvage pathway
- 2. The pathways for the biosynthesis of the amino acidsglutamine (Gln) and proline (Pro) involve one or morecommon intermediates. Auxotrophic yeast mutantsnumbered 1–7 are isolated that require either glutamine or proline or both amino acids for their growth,as shown in the following table (+ means growth; −no growth). These mutants are also tested for theirability to grow on the intermediates A–E. What is theorder of these intermediates in the glutamine and proline pathways, and at which point in the pathways iseach mutant blocked?Gln +Mutant A B C D E Gln Pro Pro1 + − − − + − + +2 − − − − − − + +3 − − + − − − − +4 − − − − − + − +5 − − + + − − − +6 + − − − − − + +7 − + − − − + − +2. Blue-green algae (cyanobacteria) form heterocysts when deprived of ammonia and nitrate. In this form, the algae lack nuclei and are attached to adjacent vegetative cells. Heterocysts have photosystem I activity but are entirely devoid of photosystem II activity. What is their role? 3. Several classes of LDL-receptor mutations have been identified as causes of this disease. Suppose that you have been given cells from patients with different mutations, an antibody specific for the LDL receptor that can be seen with an electron microscope, and access to an electron microscope. What differences in antibody distribution might you expect to find in the cells from different patients?1. Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis? 2. Some plants contain compounds that inhibit serine proteases. It has been hypothesized that these compounds protect the plant from proteolytic enzymes of insects and microorganisms that would damage the plant. Tofu, or bean curd, possesses these compounds. Manufacturers of tofu treat it to eliminate serine protease inhibitors. Why is this treatment necessary?
- 6. What is a glycosyltransferase? Choose all that apply Group of answer choices Catalyzes the formation of a bond between a sugar and an amino acid An enzyme that cleaves a glycosidic bond An enzyme that catalyzes the formation of a glycosidic bond An enzyme that transfers nucleotide-sugars from the cytoplasm 7. Which statement(s) is/are true about inverting and retaining glycosyltransferases? a. Inverting glycosyltransferase catalyzes the epimerization of a sugar b. Inverting glycosyltransferase alters the anomeric configuration of the glycosyl donor c. Retaining glycosyltransferase never preserves the anomeric configuration of the glycosyl donor d. Inverting glycosyltransferase switch the order of acceptor and donor. e. An SN1 reaction mechanism results in exclusive retention of stereochemistry of the anomeric carbon5. What is the effect of CuSO, on the enzymatic activity of catalase? 6. Is CuSO4 an activator or inhibitor? If it is an inhibitor, what kind of inhibitor is it?1. We saw how evolution has led to the existence of protein families composed of related molecules with similar functions. A few examples are also known where proteins with very similar functions have primary and tertiary structures that show no evidence of evolutionary relationship. Subtilisin and trypsin, for example, are two protein-digesting enzymes (proteases) that show no evidence they are homologous despite the fact that they utilize the same mechanism for attacking their substrates. How can this coincidence be explained? 2. Would you agree with the statement that many different amino acid sequences can fold into the same basic tertiary structure? What data can you cite as evidence for your position. 3. In the words of one scientist: “The first question any structural biologist asks upon being told that a new [protein] structure has been solved is no longer ‘What does it look like?; it is now What does it look like?’” What do you suppose he meant by this statement?