2. Draw the chemical mechanism for the addition of an RNA nucleotide triphosphate to a growing RNA transcript. Be sure to explicitly show the attacking nucleophile and the leaving group, and every covalent bond that gets formed and broken in the reaction.
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- 19. Nucleic acid structures can form supercoils in the cell. Why is it necessary to form supercoils in the cell? What type of supercoils exist in the cell? What enzymes resolve these supercoils and briefly describe the enzymatic mechanism for resolving supercoils?8. Which of the following is NOT true about polypeptides? The peptide bond that links the amino acids together is a type of covalent bond formed through dehydration synthesis. If the overall isoelectric charge of a polypeptide is negative, it will be pulled towards the cathode end during gel electrophoresis. The polypeptide chain modified with ubiquitin molecules are tagged for proteasomal degradation ○ In prokaryotic translation, the initial polypeptide chain produced has a formylmethionine amino acid at the N- terminal.22. Oxidative deamination of adenine leads to an A•T → G•C transition mutation. How does adenine become deaminated? Please draw the reaction mechanism of this deamination reaction in at least 2 steps. Also, explain how this occurs by drawing the resulting base pair formed. H. 'N' N. HNO2 N. R
- 3. Solve the sequence of an oligopeptide 7 residues long which gave: Asp Leu Lys Met Phe Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. The PTH derivative from Edman degradation was c. Brief chymotrypsin treatment yielded several products including but not limited to a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and a free Lys.Protease enzymes cleave proteins by hydrolyzing peptide bonds. The strategy for each type of metalloprotease begins with generating a nucleophile that attacks the peptide bond that attacks the peptide carbonyl group. O Macmillan Learning On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a metalloprotease. Metalloproteases H R₁ HN Zn Enz 2+ R₂ Draw curved arrows on the pre-drawn structures to show the metalloprotease mechanism. If you need to reset the structures, click More followed by Reset Drawing. Select Draw Templates Groups More B - H Enz H H с R1 | : HN O | Zn 2+ B R2 N Zn Erase3. Show the Hydrolysis of a dipeptide containing the amino acids threonine and methionine. rotta
- S1.What functional group (pictured below) is used in the formation of ATP, the backbone of DNA, and the plasma membrane? R. - HO- asluolom OgH 910m ansa obyd to inuoms adisi69 101 P- Hnedenoi HO 9tom anisinos H 19w 1639 eniv blut viend ou nontel:oceansied bol-ngtsl s19 1591 a. Amino b. Carbonyl c. Ester d. Phosphate e. Alcohol Sabios onime Tertio of bensemoo Insietib ti aolem tsrll blas onims ns to neg at to quang ly snodibod for ogh quotg3. Below is the structure of a nucleotide triphosphate. ATP R-O- R-O R-O- OIP O P -O O OP ADP OIPIO b. a. Label each phosphate group as a, ß, or y in boxes provided below each phosphate group. Put an "X" under all products you would expect from nucleophilic attack at the y phosphate group by a generic alcohol (R-OH). fofo O H R-O O. H Adenosine R-O OH fof O O=P O O H R-O-Adenosine H OH OIPIO NH₂ O-AMP AMP N O=0 O-Adenosine3. Solve the sequence of an oligopeptide 7 residues long which gave: Asp Leu Lys Met Phe Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. The PTH derivative from Edman degradation was c. Brief chymotrypsin treatment yielded several products including but not limited to a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and a free Lys. Instructions Make use of the table below to determine the sequence of the mystery protein.
- 9. In pre-historic earth, where there exist no protein enzyme, ribozymes (ribose enzymes) seems to play their roles as catalysts. Rationale why they can be catalysts, while their precedent molecule DNA cannot be catalysts.2. A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete hydrolysis of a hexapeptide. a. Edman’s reagent releases leucine b. Hexapeptide with carboxypeptidase releases serine. c. Hexapeptide with trypsin forms a tripeptide A with leucine at the N terminal and tripeptide B with valine at the N terminal. d. Tripeptide A with carboxypeptidase releases arginine and a dipeptide with glutamic acid at C terminal. e. Tripeptide B with chymotrypsin form releases serine and another dipeptide. Give: 1. the amino acid sequence of tripeptide A and B. 2. the amino acid sequence in the above hexapeptide.1. Draw and define the following terms: Binding Site Catalytic Site Allosteric Site Conformational change