Fill in the blanks: In the given reaction below, the amino acid HN NH₂ OH N. HN- undergoes NH₂2 reaction.
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A: Amino acid inhibitors are molecules that can interfere with the function of specific amino acids by…
Q: Why is it that not all the angles between C-N can freely rotate?
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Q: One strand of a double-helical DNA has the sequence 5'-GCGCAATATTTCTCAAAATATTGCGC-3'. Write the base…
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Q: mechanism and what we learned about acid/base chemistry, why chymotrypsin would not be able to…
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Q: Write note on mutarotation.
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Q: How does Stoichiometry in Chemical Reactions relate to our daily life activities? How also relevant…
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Q: Cellular location where TCA Cycle reactions occur. O Cytoplasm Endoplasmic Reticulum Mitochondrial…
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Q: Define enzymes. Explain nomenclature and IUBMB classification with suitable examples.
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Q: How is the PDHC regulated?
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Q: What does ‘separation of bound from free’ mean in terms of the radioimmunoassay?
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Q: In no more than 100 describing a negative control that you might perform along side your dna…
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Q: need to now the migration distance for protein A and and also the distance fort protein B please
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Q: Fill in the blanks: In the given reaction below, the amino acid CH3 H₂C-N* CH₂ NH₂ B KMTS undergoes…
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Q: In follow up would it be possible to do part D and E in the question as well?
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Q: Please use the graph below to explain the differences between the 2 enzymes whose activities are…
A: Enzymes are biocatalysts that increases the rate of a reaction by bringing down the activation…
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- Question 9. Which of thefollowing is not formed through adehydration synthesis reaction?A. polysaccharideB. polypeptideC. Nucleic acidD. phospholipidE. glycerolQUESTION 22 When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Allosteric activation Zymogen activation Covalent modification Competitive inhibition Allosteric inhibitionQuestion 10. All of the following areparts of a nucleotide EXCEPT:A. a five-carbon sugar.B. a six-carbon sugar.C. a phosphate group.D. a nitrogenous base.
- QUESTION 4 According to the Arrenhius theory, an acid is: a. a substance that forms hydroxide ions b. a proton donor c. a substance that forms hydronium ions d. a proton acceptorQuestion 1: When the CAC is run in reverse by microorganisms that use it to fix carbon, the citrate synthase reaction is different and is catalyzed by an enzyme called ATP-citrate lyase. Write the reaction catalyzed by ATP-citrate lyase, then briefly (in one sentence) explain why the use of different chemistry (different from the ‘normal’ direction) makes sense here.question: 4. in the diagrams below, what type of solution is each cell?
- Question 22: which of the following secondary structures would you expect to find on the surface of a globular protein? Alpha helix Beta sheet Loops between two alpha-helices None of the above because water would disrupt the hydrogen bonding that stabilizes these structures A,B and C as long as the polar and charged amino acid side chains face the surface of the protein.Question 10 (2 points) A protein heterodimer would be considered an example of: -primary structure -secondary structure -tertiary structure -quaternary structure -atomic structureQuestion #6 Part A. What do Serine, Threonine, and Tyrosine have in common? Part B. How would the addition of a phosphate group change the chemical behavior of those amino acids listed in part A?
- Question 4. If you were to synthesize a tetrapeptide consisting of all alanine residues, you would have how many bonds between carbon and nitrogen?Question 1. A "relaxed" animal conserves its glycogen and oxygen, and in this way lactic acid can be produced enzymatically, which naturally softens the meat, favors its softening and makes it easier for other enzymes to synthesize compounds responsible for aroma and flavor True or false Question 2: For the Maillard reaction to occur, _____ a and ______ a group part of an amino acid or protein . a. reducing sugar, amino b. amino sugar, hydroxyl c. Ketosis, Ketone, D. aldose, phosphateQuestion 1: Part a: Assume that the standard free energy of ATP hydrolysis is -31 kJ/mol. Assume the following values for the standard free energy changes of the four reactions: HK -16.7 kJ/mol; PFK -14.2 kJ/mol; PGK -18.9 kJ/mol; PK -31.7 kJ/mol. (from bio.libretexts.org). Use these values to compute the standard free energy of hydrolysis (releasing Pi) of i. glucose 6-P ii. fructose 1,6-bis-P iii. 1,3-bisphosphoglycerate iv. phosphoenolpyruvate Part b: Which of these four compounds is the strongest phosphoryl donor?______________ Which is the weakest?__________________ Part c: The phosphoglycerate kinase reaction is favorable by -18.9 kJ/mol in the glycolytic direction, as stated above. In gluconeogenesis, this step is simply reversed; i.e. it is not one of the three steps in gluconeogenesis that is driven by using different chemistry than that of glycolysis. How can this be? (Be specific: what specific factors could enable reversal of this step?)