11- During the acid hydrolysis of a protein (6N HCl at 110°C for 24, 48 and 72hours) to determine the amino acid composition:a- Serine and Threonine are completely destroyed at all time points and cannotbe quantitated.b- Tryptophan is completely destroyed at all time points and cannot bequantitated.c- Asparagine and Glutamine are slowly converted to Aspartate and Glutamateand a time course correction must be used.d- Histidine is slowly destroyed and a time course correction must be used.e- Peptide bonds involving hydrophobic residues are slowly hydrolyzed andtime course analysis must be used.Which of the above statements are true?

The acid hydrolysis of protein is generally carried out using strong acid like HCl that breaks the…

Answered: 11- During the acid hydrolysis of a…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter19: The Tricarboxylic Acid Cycle

Section: Chapter Questions

Problem 20P

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1. In a protein, why does when Ala is replaced with Ile, it loses its activity but when Lys is replaced by Arg and Leu to Ile, it only has little effect on protein structure and function? Explain. 2. Why do proteins cannot be denatured reversibly when they are chemically altered to change the chemical composition of certain side chains? Explain.
1. Hemoglobin researchers have discovered more than 500 naturally occurring hemoglobin mutations. The majority of these results from single amino acid changes. Some of these mutations result in clinical illness or symptoms, but many show no outward effects. Some examples are: HbS (sickle cell Hb)-substitutes Val for Glu on the surface Hb Cowtown - eliminates an ion pair used in T-state stabilization Hb Memphis - surface uncharged polar aa for another of similar size on the surface Hb Bibba-substitutes a Pro for a Leu in an α-helix Hb Milwaukee - substitutes a Glu for a Val Hb Providence- substitutes a Asn for a Lys that normally projects into the central cavity Hb Philly - substitutes a Phe for a Tyr, disrupting hydrogen bonding at the aß interface. EXPLAIN your choices for each of the following: a) The Hb variant least likely to cause pathological symptoms b) The variant(s) most likely to show pl values different from that of HbA c) The variant(s) most likely to show…
1)De novo synthesis of nucleotides is an energy intensive process and therefore not always the primary source of nucleotides.Explain what is meant by this statement and how the process is regulated(specifically for urines)
6. Several human lysosomal storage diseases result from mutations in the enzymes responsible for breakdown of glycosphingolipids leading to toxic buildup of the uncleaved substrate. Similar buildup of glycosphingolipids sometimes occurs even when there is ample enzyme present. Explain how this could happen.
7. During amino acid catabolism, how is amino group removed and excreted in the form of urea? Please write the reactions starting from a generic amino acid to the formation of urea. Please indicate the names of enzymes, cofactors, names of substrates, and products of each reaction and the location of the reaction i.e. whether in cytoplasm or mitochondria.
18) Based on your knowledge of lactose system in prokaryotes) and considering the following genotypes, complete the table below indicating a "+" where an enzyme is produced and a where no enzyme is produced. Note: Is is a mutant that cannot recognize allolactose
11) After feeding at the surface of the ocean during the day, many ocean organisms migrate to deeper waters. While there, they release ammonia in their urine. Many bacteria use the nitrogen from the ammonia as they make amino acids, which eventually end up in food chains on both land and water. These amino acids may even be used in humans. Which statement best explains these observations?
15. The free energy of folding of a protein is -17kJ/mol. What tenoerature (C) do you have to heat the protein to unfold 10% of the proteins in solution?
1. Doesn't non-fat milk protein contain casein which interacts with the Bradford reagent. why would this react with the Bradford or Bruiet reagent? 2. Tryptophan is an amino acid and there should not be a reaction with the reagent. Why would there be a reaction with the Bradford or Biuret reagent?
3. In studying normal and mutant forms of a particularhuman enzyme, a geneticist came across a particularly interesting mutant form of the enzyme. Thenormal enzyme is 227 amino acids long, but themutant form was 312 amino acids long. The extra85 amino acids occurred as a block in the middleof the normal sequence. The inserted amino acidsdo not correspond in any way to the normal proteinsequence. What are possible explanations forthis phenomenon? How would you distinguishamong them?
don't copy 6. A protein-ligand binding reaction is run. At equilibrium, half the protein is ligand bound, the unboundligand concentration is 0.657 nM. Calculate the koff value for this reaction. Assume the kon value is typical ofprotein-ligand interactions.
9. Many protein modifications take place in the endoplasmic reticulum (ER). Name one ER enzyme (and state its role) that functions to modify a protein.

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