pls complete this with in 15 min 2. Use your knowledge of amino acids (and the R groups) and tertiary structures of proteins toexplain how the simple change of one base in the DNA that causes the change in an amino acidcan lead to sickle cell anemia. Must be in your own words

Sickle cell anemia is a inherited disorders due to defect in the gene. In this disease mutation…

Answered: 2. Use your knowledge of amino acids…

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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4. Draw and name the covalent linkage between two deoxynucleotides. Indicate both the 5’ and 3’ end. You should include all relevant atoms, though for the bases you may simply put the one-letter abbreviation instead of a drawing.
3. Approximate molecular weight for an unknown protein from gel-filtration experiment is 130 kDa. Thirty six mg of this pure protein was treated with excess of fluorodinitrobenzene. After the reaction and complete acid hydrolysis the mixture was found to contain 356 µg of dinitrobenzene derivative of methionine (free acid) and no other amino acid-dinitrobenzene derivatives. Is this protein consisting of single polypeptide chain or multiple subunits? If it consists of multiple subunits, then how many? From these data, can you calculate the molecular weight of the protein more precisely?
1. The protein illustrated below was isolated from a superhuman being. Scientists theorized that it was the source of power of its power. CH3 NH но CH3 NH NH NH NH NH NH HO H. NH H3C H3C H3C NH2 a. Construct the sequence of the protein using the three letter symbol.
10. A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the physiological protein has a molecular weight of 240,000 Daltons. Chromatography in the presence of 6 M urea yields a single peak corresponding to a protein of 60,000 Daltons. Chromatography in the presence of 6 M urea and 10 mM mercaptoethanol yields peaks for proteins of 34,000 Daltons and 26,000 Daltons. What can we learn about protein's tertiary and quaternary structure from this data?
1. In DNA, which chemical processes result in the formation of 3'-5' phosphodiester bond and C1 sugar-base bond, respectively? Do condensation and glycosidic bond take place? 2. H bond plays vital role for the stability of protein secondary structure. Similarly, are there any specific force/bonding that is the most important for tertiary and quarternary structure, respectively? If there is, what are they?
27. The A-T base pair has more hydrogen bonding than the C-G base pair. True False
1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?
2. As we've seen previously, peptide bonds involving the amino acid proline can populate both "trans" and "cis" isomers. trans-Pro cis-Pro This isomerization reaction can be the rate-limiting step in protein folding. Depending on the protein sequence, the relative favorability of the trans and cis states can change. For Pro-117 in the protein staphylococcal nuclease, the rates of the forward and reverse reactions are: ktrans→cis = 3.1 × 10-2 and kcis→trans = 2.5 x 10-3 s-1. (a) What is AG°' for this reaction? (b) A prolyl isomeriase enzyme increases the rate of the forward reaction to kcat.trans->cis = 2.6 s-1. What is the new rate constant for the reverse reaction (kcat,cis→trans)? (c) This prolyl isomerase is a Michaelis-Menten enzyme with kcat = 2.6 s!, KM = 1.9 µuM. If you have 1 nM enzyme, what is Vo for [S]o = 0.7 µM? What about [S]o = 30 µM? For each condition, what limits the reaction speed?
4. A hypothetical protein has a molar mass of 23,300 Da. Assume that the average molar mass of an amino acid is 120. How many amino acids are present in this hypothetical protein? What is the minimum number of codons present in the mRNA that codes for this protein? What is the minimum number of nucleotides needed to code for this protein?
3. Choose one of the following structures (a or b) to draw. a) Draw the basic structure of a nucleotide that is found only in RNA. Use 'P' for the phosphate (or try to draw this functional group if you wish). You must correctly draw the sugar/ribose, and include the appropriate nitrogenous base attached at the correct location. OR b) Draw the basic structure of the polysaccharide amylose (starch) - only include 3 monosaccharides within this chain. You do not need to draw the 'C' atoms within the ring, unless you want to. If you wish to leave the hydrogen atoms out that is fine, but make sure to include all functional groups and important bonds.
3. Choose one of the following structures (a or b) to draw. a) Draw the basic structure of a nucleotide that is found only in RNA. Use 'P' for the phosphate (or try to draw this functional group if you wish). You must correctly draw the sugar/ribose, and include the appropriate nitrogenous base attached at the correct location. OR b) Draw the basic structure of the polysaccharide amylose (starch) - only include 3 monosaccharides within this chain. You do not need to draw the 'C' atoms within the ring, unless you want to. If you wish to leave the hydrogen atoms out that is fine, but make sure to include all functional groups and important bonds. 4. Illustrate with diagram(s) the process of competitive inhibition. Your labels and a brief description will be enough to summarize the process perfectly.
2. Show the Dehydration Synthesis reaction that occurs to form a tripeptide containing the following amino acids: valine, glycine and alanine

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2. Use your knowledge of amino acids (and the R groups) and tertiary structures of proteins to explain how the simple change of one base in the DNA that causes the change in an amino acid can lead to sickle cell anemia. Must be in your own words