Homework Answers
Answer:
B. Lysine
Explanation: Methionine, Threonine and isoleucine can derive their carbon skeleton from the succinyl Co-A , a substrate in the kreb cycle formed from the products of the Oxaloacetic acids.
Lysine is derived from outside the kreb cycle, from the acetoactyl Co-A.
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QUESTION 10 An amino acid that does not derive its carbon skeleton, at least in part,...
An amino acid that does not derive its carbon skeleton, at least in part, from aspartate?...
An amino acid that does not derive its carbon skeleton, at least in part, from aspartate? OA isoleucine, B-lysine, Cmethionine, D.proline, E.threonine. OF. all of the above derive some carbon from OAA. QUESTION 11 The coenzyme involved in a transaminase reaction is? A. tetrahydrofolate (FH4) B. lipoic acid, OC. nicotinamide adenine dinucleotide phosphate (NADP+), OD.pyridoxal phosphate (PLP), O E. thiamine pyrophosphate (TPP), OF. none of the above. 12 Which lipoproteins pick up cholesterol from non-liver tissues, including foam cells at...
Easy questions, 30 min timed assignment, please answer ASAP thanks. The amino acid least likely to...
Easy questions, 30 min timed assignment, please answer ASAP thanks.
The amino acid least likely to be involved in nucleophilic a. Alanine. b. Asparagine. 1. and/or electrophilic enzyme catalysis is e. All are equally likely c. Aspartate. d. Arginine Fibrous proteins, such as collagen, have which one of the following properties? a. b. c. d. e. 2. highly soluble in water their hydrophilic residues are directed into the interior of the protein exhibits enzymatic activity serve structural roles in the...
Which of the following does not provide a carbon skeleton for the synthesis of amino acids?...
Which of the following does not provide a carbon skeleton for the synthesis of amino acids? Select one: a. Succinate. b. α-Ketoglutarate. c. Pyruvate. d. Oxaloacetate. e. Ribose 5-phosphate.
1)Match the name of each amino acid with one of its characteristics. 2)has a hydroxy group...
1)Match the name of each amino acid with one of its characteristics. 2)has a hydroxy group its aromatic side chain 3)has a sulfur atom in its side chain that can form disulfide bonds its side chain is a nonpolar isopropyl group 4)it has the smallest acidic side chain 5)this amino acid has the smallest side chain of all, a hydrogen atom 6)its side chain is a methyl group its side chain of 3 carbons forms a 5-membered ring with the...
Question 6 2 pts Some amino acids can supply the carbon required for gluconeogenesis by undergoing...
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Question 10 (10 pts) Peptides are biological oligomers formed by condensing multiple amino acids into an...
Question 10 (10 pts) Peptides are biological oligomers formed by condensing multiple amino acids into an amide backbone. Although this amide backbone is common to all peptides, the so- called 'side-chan' groups attached to this backbone vary depending the amino acids used in the condensation reaction. Shown below are four different tetrapeptides (so-named because they are the products of the condensation of four amino acids). Based on their structures, predict the order of elution that one might expect if separating...
1. When amino acids are degraded the first step is to remove the amino group. To...
1. When amino acids are degraded the first step is to remove the amino group. To which of the following molecules is the amino group typically transferred? A. Pyruvate B. Oxaloacetate C. Fumarate D. Alpha-ketoglutarate 2. Most amino acid degradation takes place in the ... A. Adipose B. Muscle C. Liver D. Epithelium 3. Urea contains two nitrogen atoms. What is the source of these two nitrogen atoms? A. Both from NH4+ B. NH4+ and aspartate C. NH4+ and serine...
17. Which of these amino acids has a thiol group as part of its side chain?...
17. Which of these amino acids has a thiol group as part of its side chain? a. cysteine tyrosine Aca histidine threonine e: alanine 18. Which structure correctly represents an amino acid zwitterion? C- OH. NH R CH C- OH NH, NH R- CHHC OH NH NH
TABLE 5.1 PK values for amino acids 2.36 Amino acid Alanine Arginine Asparagine Aspartic acid Cysteine...
TABLE 5.1 PK values for amino acids 2.36 Amino acid Alanine Arginine Asparagine Aspartic acid Cysteine Glutamic acid Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine PK, PK₂ 2.34 9.69 2.17 9.04 2.02 8.80 1.88 9.60 1.96 10.28 2.19 9.67 2.17 9.13 2.34 9.60 1.82 9.17 9.60 9.60 2.18 8.95 2.28 1.83 9.13 1.99 10.60 2.219.15 2.09 9.10 2.83 9.39 2.20 9.11 2.32 9.62 2.36 9.21 5.56. Of the amino acids listed in Table...
how does the protein environment surrounding an amino acid chain affect its chemical properties?Consider the carboxyl...
how does the protein environment surrounding an amino acid chain affect its chemical properties?Consider the carboxyl group on an asparate side chain in the following environments in a protein. Rank in order these environments from the highest to the lowest proportion of carboxyl groups in the -COO- form.that is in terms of pKas. 1. an aspartate side chain on the surface of protein with no other ionizable groups nearby. 2. an aspartate side chain buried in a hydrophobic pocket on...
An amino acid that does not derive its carbon skeleton, at least in part, from aspartate? OA isoleucine, B-lysine, Cmethionine, D.proline, E.threonine. OF. all of the above derive some carbon from OAA. QUESTION 11 The coenzyme involved in a transaminase reaction is? A. tetrahydrofolate (FH4) B. lipoic acid, OC. nicotinamide adenine dinucleotide phosphate (NADP+), OD.pyridoxal phosphate (PLP), O E. thiamine pyrophosphate (TPP), OF. none of the above. 12 Which lipoproteins pick up cholesterol from non-liver tissues, including foam cells at...
Easy questions, 30 min timed assignment, please answer ASAP thanks.
The amino acid least likely to be involved in nucleophilic a. Alanine. b. Asparagine. 1. and/or electrophilic enzyme catalysis is e. All are equally likely c. Aspartate. d. Arginine Fibrous proteins, such as collagen, have which one of the following properties? a. b. c. d. e. 2. highly soluble in water their hydrophilic residues are directed into the interior of the protein exhibits enzymatic activity serve structural roles in the...
Question 6 2 pts Some amino acids can supply the carbon required for gluconeogenesis by undergoing a reaction catalyzed by an aminotransferase, an enzyme that interconverts amino acids and -keto acids. Aspartate aminotransferase catalyzes the reaction shown below. aspartate + a-ketoglutarate - oxalacetate + glutamate A biochemist studying metabolism feeds 4-[14C]-aspartate (asparatate that has 14C, the radioactive isotope of carbon, at the sidechain carboxylate) to his rats. After sacrificing the rats he is unable to find any +4C in glucose....
Question 10 (10 pts) Peptides are biological oligomers formed by condensing multiple amino acids into an amide backbone. Although this amide backbone is common to all peptides, the so- called 'side-chan' groups attached to this backbone vary depending the amino acids used in the condensation reaction. Shown below are four different tetrapeptides (so-named because they are the products of the condensation of four amino acids). Based on their structures, predict the order of elution that one might expect if separating...
17. Which of these amino acids has a thiol group as part of its side chain? a. cysteine tyrosine Aca histidine threonine e: alanine 18. Which structure correctly represents an amino acid zwitterion? C- OH. NH R CH C- OH NH, NH R- CHHC OH NH NH
TABLE 5.1 PK values for amino acids 2.36 Amino acid Alanine Arginine Asparagine Aspartic acid Cysteine Glutamic acid Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine PK, PK₂ 2.34 9.69 2.17 9.04 2.02 8.80 1.88 9.60 1.96 10.28 2.19 9.67 2.17 9.13 2.34 9.60 1.82 9.17 9.60 9.60 2.18 8.95 2.28 1.83 9.13 1.99 10.60 2.219.15 2.09 9.10 2.83 9.39 2.20 9.11 2.32 9.62 2.36 9.21 5.56. Of the amino acids listed in Table...
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