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- QUESTION NO.1which of the following are chemical characteristics of monosaccharides? A. They contain multiple hydroxyl groupsB. they contain an aldehyde or ketone group C. They contain a branching carbon backbone D. They contain a carbon-carbon double bond E. Every carbon in a monosaccharide is fully reduced F. Every carbon in a monosaccharide is a chiral centerQUESTION NO.2 glucose absorption is hindered by _________ deficiency A. Retinol B. Thiamine C. Potassium D. Sodium E. Ascorbic acid F. Calciferol QUESTION NO.3 phospholipids is made primarily from A. L-glycerol 1-phosphate B. L-glycerol 3-phosphate C. D-glycerol 3-phosphate D. -glycerol 1-phosphate E. sn-glycerol 1-phosphate F. sn-glycerol 3-phosphateQUESTION NO. 1L-Carnitine is synthesized primarily in the liver but also in the kidneys and then transported to other tissues. It is most concentrated in tissues that use fatty acids as their primary fuel, such as skeletal and cardiac muscle. In this regard, L-carnitine plays an important role in energy production by conjugating to fatty acids for transport from the cytosol into the mitochondria. L-carnitine shuttle is an example of A. ion driven active transport B. facilitated diffusion C. simple diffusion D. ATP driven active transportE. symport F. antiportQUESTION NO.2 Statements: (1) Glucose is both a hexose and a aldose. (2) There can never be more than three enantiomers for a molecule. (3) All common disaccharides have beta-one-four linkages. Which statements are true?QUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibition
- Question:- 33) Glucose-6-phosphate has different pathways that it can enter in the liver during the fed state. All of the following are possible except OA.) it is oxidized to acetyl CoA for fatty acid biosynthesis O B). it can enter the pathway for glycogen biosynthesis O c.) it is a substrate for glucose-6-phosphatase OD. )it is oxidized in glycolysis to provide energy for the bodyQUESTION 16 Peptidyl transferase activity (peptide bond enzyme activity) is associated with what site in the ribosome? E P A XQuestion 1: ATP synthases contains 3 copies of each of the large subunits (called α and β in the E. coli enzyme). The number of c subunits can vary among different ATP synthases, ranging from 8 to 17. Part a: Briefly explain how this variation in the number of c subunits would affect the energetics of ATP synthesis. For a fixed value of the protonmotive force, how much energy can the gradient provide to drive one revolution of the ATP synthase, in a synthase with 8 c- subunits versus a synthase with 17 c-subunits?
- Question 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.question 38 The constant region of each heavy chain determines the class of the heavy chain. True FalseQuestion 11. // Hint: Isoelectric focusing separates proteins based on their pI values, and can separate proteins that only differ by a net charge of ±1.±1. Recall that an amino acid residue with a negatively charged R group has a relatively low isoelectric point (pI) where it has zero net charge. Likewise, an amino acid residue with a positively charged R group has a relatively high isoelectric point (pI) where it has zero net charge. Order from Low pH to High pH
- QUESTION NO. 1Targeting a protein to be degraded within proteasomes usually requires ubiquitin. In the function of ubiquitin all of the following are true except: A. ATP is required for activation of ubiquicin. B. a peptide bond forms between the carboxyl terminal of ubiquitin and an ε-amino group of a lysine . C. linkage of a protein to ubiquitin does not always mark it for degradation. D. the N-terminal amino acid is one determinant of selection for degradation. E. ATP is required by the enzyme that transfers the ubiquitin to the protein to be degraded QUESTION NO. 2Much of procollagen formation occurs in the endoplasmic reticulum and Golgi apparatus which requires signal peptide. All of the following statements about targeting a protein for the ER are true except. A. signal peptide usually has a positively charged N-terminus and a stretch of hydrophobic amino acids. B. signal peptide emerging from a free ribosome binds signal recognition…QUESTION 21 You are in charge of generating a scaffold for use in tissue engineering applications that behaves similarly to the natural ECM proteins. What proteins might you want to include in your scaffold? A Fibronectin only B Collagen, fibronectin, and proteoglycans C Proteoglycans only D None of the above are proteins in the ECM E Collagens onlyQuestion 1: The 4 kinase steps in glycolysis are catalyzed by hexokinase, phosphofructokinase, phosphoglycerate kinase, and pyruvate kinase. Write each of these four reactions, including all participants. i. ii. iii. iv.