5. ANSWER THE FOLLOWING PROBLEM AND EXPLAIN YOUR ANSWER FOR BETTER UNDERSTANDING. Fill in the blanks In the given reaction below, the amino acid histidine undergoes transmethylat reaction. HN- NH₂ OH HN NH₂
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- 1. To determine the sequence of amino acids in protein, partial hydrolyses at different points are made and then compared to other sets of partial hydrolyses For example: Complete hydrolysis gave: Phenylalanine-1 Histidine-2 Glutamic acid-1 Leucine - 4 Asparagine-1 Cystine -2 Glutamine-1 Glycine - 2 The Partial Hydrolyses yielded the following: 1st Hydrolysis : 4 polypeptides ● . IA: phe-val-asn-gln-his-leu IB: IC: leu-tyr-leu-val ID: val-cys-gly 2nd Hydrolysis: 3 polypeptides IIA: phe-val-asn-gIn-his-leu-cys-gly-ser-his-leu IIB: val-glu-ala-leu-tyr-leu IIC: val-cys-gly Write down the primary structure of this polypeptide by finding the overlaps of the amino acids therein: Serine-1 Valine-3 Alanine-1 tyrosine-1 cys-gly-ser-his-leu-val-glu-ala1. You need 0.5 liter of a 0.1 M buffer for a biochemical reaction that you plan to perform at pH 2.0. On the shelf in your laboratory you have available phosphoric acid, and the amino acids aspartate, glycine, glutamate, tyrosine, and histidine (all you have available are the fully deprotonated forms of the molecules); these are the only buffer materials you have available. (The pKa values for these compounds are given below.) For phosphoric acid, pKal1 = 2.12, pKa2 = 7.21, and pKa3 = 12.32 For aspartate, pKaCOOH = 1.88, pKaNH3+ = 9.60, pKa sidechain = 3.65 For glycine, pKaCOOH = 2.34, pKaNH3+ = 9.60 For glutamate, pKaCOOH = 2.19, pKaNH3+ = 9.67, pKa sidechain = 4.25 For histidine, pKɑCOOH = 1.82, pKɑNH3+ = 9.17, pKa sidechain = 6.00 For tyrosine, pKaCOOH = 2.20, pKaNH3+ = 9.11, pKa sidechain = 10.07 a. Of these possible buffers, which is likely to yield the greatest resistance to pH change from the starting pH of 2.0, assuming that you were going to run a biochemical reaction that…2. Serine is an uncharged, polar amino acid (below and left). Threonine (below and right) is another uncharged, polar amino acid. Illustrate the hydrolysis of a dipeptide that was made from these two amino acids. Be sure to write all involved reactants and products in the structural form like Serine, and as a proper chemical equation; eg. reactant(s) – product(s). Your diagram of the dipeptide must show the N-terminal and C-terminal ends at opposite sides of the dimer molecule, and you need to indicate where the peptide bond is with an arrow/highlighter. H c-C-N OH NH2 CH,-CH -C-COO но CH. он H
- Copy of The following reaction scheme shows the states of the amino acid hisitdine. Histidine has three pKa's - 2, 6 and 9.2. Which form of Histidine predominates at pH of 5? *H3N-CH-Ĉ-OH CH2 *H3N-CH-C–O- CH2 "H3N-CH-C-O- CH2 H2N-CH-C–O- CH2 +HN *HN N' -NH -NH -NH NH A C O A. A ОВ. В OC.C O D.D O E. The answer cannot be determined with information given.Describe the tertiary level of protein structure and state the type of interactions present.14. With the aid of diagrams, explain the difference between spontaneous and nonspontaneous enzyme reactions15. Briefly explain how enzymes decrease the activation energy of biochemical reactions.16. What is the difference between a nucleoside and a nucleotide?17. A nucleic acid has 13% of adenine. Determine the composition of guanine, cytosine and thymine.1. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 7? 2. Draw the tetrapeptide Met-Ala-Thr-Thr at a ph of 12?
- Please draw a single polypeptide chain structure that has the following amino acids (leucine, alanine, cystine, argenine, glutomine, and leucine) as it would appear at physiological pH. Calculate the pl of the polypeptide. I will rate!Using abbreviations (not structures), write the reaction of flavin adenine dinucleotide that gives off energy (-AG). Match the items in the left column to the appropriate blanks in the equation on the right. H+ FADH → FADH3 + H+ 3/2H2 FADH3 FAD FADH 2H+ FADH2 3H+ H23) Type 1 EA can be done on both and functional groups. Complete the sentence above. Explain what the difference is in the products for each functional group used.
- H8. Protein A interacts with biomolecule B and forms a complex AB, with a dissociation constant KD = 1 µM at 25 °C, (for dissociation, AB ⇋ A + B, KD=[A][B]/[AB]). The interface contains a phenylalanine residue. A biochemist mutated the phenylalanine of protein A to a tyrosine (A’), which introduced a hydrogen bond between the hydroxyl group of the tyrosine with B without affecting any other interactions. The formation of the hydrogen bond releases a heat at 11.4 kJ/mol. What is the KD of the complex of the mutant A’ with B? Hint: Gas constant R = 8.3145 J/K/mol, Euler’s number e = 2.7183, ln(A) - ln(B) = ln(A/B).Would you consider the formation of a peptide bond to be an example of a neutralization reaction? Explain your reasoning. 1. *2. Amino acid analysis of the a heptapeptide gave the following residues: Asp Glu Leu Lys Met Tyr Trp NH4+. The following facts were observed: Trypsin treatment had no effect. The phenylthiohydantoin released by Edman degradation was OH H C-C-CH₂ H. Brief chymotrypsin treatment yielded several products including a dipeptide and a tetrapeptide. The tetrapeptide contained Glu, Leu, Lys and Met is some order. Cyanogen bromide treatment afforded a tetrapeptide that had a net positive charge at pH 7 and tripeptide that had a zero net charge at pH 7. What is the amino acid sequence for this heptapeptide?