Question 18Match the following structural composition with the corresponding polysaccharideLinear homoglycan of glucose connected by a1-4 linkagesa. agarosev Branched glycan formed by alternating units of D-galactose and L-galactoseb. amylosev Linear sulfated chains of alternating B-D-galactopyranose and 3,6-anhydro- a-galactopyranosyl unitsc. amylopectinv Poly-B-Dmannopyranosyluronic acid and/or Poly-a-L-gulopyranosyluronic acidd. Alginatev Repeating Poly-D-galacturonic acid residuese. agaropectindeacetylated straight-chain amino-polysaccharide polymer linked in a B(1-4) type of linkagef. Pecting. carrageenanh. chitosan

Polysaccharides may be homopolysaccharides (contain a single type of monomer) or…

Answered: Match the following structural…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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QUESTION 26 During gluconeogenesis, whereby liver cells convert pyruvate to glucose, Fructose-6-phosphate (F6P) is converted to Glucose-6-phosphate (G6P). If the standard equilibrium concentrations are: [F6P] = 0.52 M and [G6P] = 1.48 M, then Keq’ is ______ and the reaction is ________. Fructose-6-P ó Glucose-6-P > 1; exergonic > 1; endergonic < 1; exergonic < 1; endergonic
Question 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. 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 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-phosphate
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 10. All of the following areparts of a nucleotide EXCEPT:A. a five-carbon sugar.B. a six-carbon sugar.C. a phosphate group.D. a nitrogenous base.
question 38 The constant region of each heavy chain determines the class of the heavy chain. True False
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 16 Peptidyl transferase activity (peptide bond enzyme activity) is associated with what site in the ribosome? E P A X
Question 4. If you were to synthesize a tetrapeptide consisting of all alanine residues, you would have how many bonds between carbon and nitrogen?
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 body
QUESTION 5 [20]Describe and compare the metabolism of carbohydrates, lipids and proteins and in your answer, explain the role of ATP. Also discuss the differences between anabolic and catabolic pathways, the regulation of metabolic pathways and the differences in metabolism between the well-fed and 1.1 Describe the structural characteristics that are common to all the amino acids that are found in mammalian proteins and draw the structure of the tripeptide Tyr-Thr-Trp in the ionic form that predominates at pH 7. Show all atoms (including hydrogens) as well as any charges as necessary. Explain the general features of amino acid side chains and the importance of associated non-covalent interactions. (1fasting state.

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