Please take advantage of our , , and for you preparation. An example of a transamination process is A. She is rushed to the hospital where she is given several doses of N-acetyl Cysteine. Methionine Answers with explanations 1. All of these Urea cycle also called ornithine cycle : a biochemical cycle in many animals including human to produce urea from ammonia.
A Keratin B Collagen C Myosin D Myoglobin Answer: c Q Which of the following protein contain a modified amino acid — desmosine? Histones are highly basic in charge since they are rich in basic positively charged amino acids such as lysine and arginine. The drug in this case, is given to decrease the degradation of which of the followings? An unknown amino acid 5. Aspartate Aspartate was discovered from Asparagus racemosus by Plisson in 1827. The remaining two amino acids Selenocysteine and Pyrrolysine are coded by two stop codons. Both a and b e.
Which one of the following is semi-essential amino acid for humans? Which amino acid, among the 20 standard protein coding amino acids, is most abundantly occurs in proteins? Multiple choice and true or false type questions are also provided. Tyrosine is degraded to acetoacetyl CoA and fumarate and is described as a A. Histidine is degraded to a-ketoglutarate and is described as a A. The amino acid from which synthesis of the protein of hair keratin takes place is A Alanine B Methionine C Proline D Hydroxyproline ans b 11. Which of the following is not an essential amino acid? Which of the following is a tri-peptide? Which of the following amino acids can covalently bind ammonia, transport and store in a non toxic form? A nucleotide consists of A.
Which of the following is an essential amino acid? Learn with multiple choice question: polar amino acids are usually found, online certificate courses with options inside the core of proteins, on the surface of proteins, at the sides of proteins, can be present anywhere in proteins with online sample interview questions and answers, competitive tests preparation for jobs hiring. This is why the active site of many enzymes contains one or more histidine residues since most of the enzymatic reactions involve exchange of protons and electrons between enzyme and substrates. Which of the following compounds you most likely expect to be elevated in the blood of the infant at birth if the mother was not treated properly? What is the molecular weight of Tryptophan? Which of the following amino acid is another component of Glutathione besides Cysteine and Glutamic acid? Tryptophan Methionine is also coded by a single codon 19. Multiple Choice Questions Solved - Amino acid Metabolism Multiple Choice Questions Solved - Amino acid Metabolism answers are given at the end of the questions Q. Which amino acid act as the precursor of nitric oxide biosynthesis in animals? Example of proteins containing selenocysteine: glutathione peroxidases, thioredoxin reductases, formate dehydrogenases, glycine reductases, selenophosphate synthetase and methionine-R-sulfoxide reductase. Tryptophan is a precursor for many compounds, the deficiencies of which can cause the said symptoms.
Which of the following statements about aromatic amino acids is correct? The patient experienced an episode of acute renal failure while in hospital and his serum creatinine rose to 2. Aspartic acid and Lysine together 4. An ambiguous amino acid d. This will pave the way for your medical degree,nursing degree, or other allied health degree. The reason is that its side chain -----. A vasodilating compound is produced by the decarboxylation of the amino acid: A Arginine B Aspartic acid C Glutamine D Histidine ans d 4.
Acetaminophen overdose is potentially life threatening because it depletes the cellular stores of Glutathione. Canavanine Concanavalin A ConA is a lectin isolated from a legume, jack bean Canavalia ensiformis Lectins are protein which specifically binds to carbohydrates. Furthermore proline produces a kink in the polypeptide. Non essential amino acids A Are not components of tissue proteins B May be synthesized in the body from essential amino acids C Have no role in the metabolism D May be synthesized in the body in diseased states ans b 6. Both a and b e.
Chymotrypsin is specific for peptide bonds containing A Uncharged amino acid residues B Acidic amino acids C Basic amino acid D Small amino acid residues ans a 14. Which of the following amino acid is sweet in taste? How amino acid residues in a protein determines the secondary and tertiary conformation? An essential amino acid in man is A Aspartate B Tyrosine C Methionine D Serine ans c 5. Which out of the following defects could be responsible for the said symptoms? Transaminase enzymes are present in A. A glucogenic amino acid is one which is degraded to A. A best described ketogenic amino acid is A. Her fingers are severely deformed secondary to rheumatoid arthritis. The enzyme trypsin is specific for peptide bonds of A Basic amino acids B Acidic amino acids C Aromatic amino acids D Next to small amino acid residues ans a 13.
Which amino acid act as the precursor of dopamine? Which of the following enzyme defect is likely to be there? Histidine Histidine has its pI near to physiological pH. Which of the following amino acids can covalently bind ammonia, transport and store in a non toxic form? Amino acid acting as a defensive molecule in plants: a. Dopamine to norepinephrine conversion Tyrosine to Dopa Dihydrofolate to Tetra hydro folate Phenyl Alanine to Tyrosine N-Acetyl serotonin to melatonin Q. Solved examples with detailed answer description, explanation are given and it would be easy to understand. An important reaction for the synthesis of amino acid from carbohydrate intermediates is transamination, which requires the co-factor: A Thiamin B Riboflavin C Niacin D Pyridoxal phosphate ans d 15. Further examination reveals red pupils. Toxins such as ammonia are not properly metabolized by the liver and can damage brain.