11. An enzyme requires a dinucleotide cofactor (shown below). Using the given letters, mark one example of each of the following on the cofactor. If a specific feature is not present above, write "NO" beside it in the list. "A" has been completed for you as an example. If you need to box a feature on the diagram to be clear what portion you are labeling, please do so. A A. An amine functional group CH3 NH2 HN B. A deoxy sugar C. Phosphodiester linkage D. A purine E. Hydrogen unable to hydrogen bond F. Anomeric carbon CH3 OH 'N' O-P-o-P-o OH OH он он но OH G. A structure able to participate in T- T stacking

11. An enzyme requires a dinucleotide cofactor (shown below). Using the given letters, mark one example of each of the following on the cofactor. If a specific feature is not present above, write "NO" beside it in the list. "A" has been completed for you as an example. If you need to box a feature on the diagram to be clear what portion you are labeling, please do so. A A. An amine functional group CH3 NH2 HN B. A deoxy sugar C. Phosphodiester linkage D. A purine E. Hydrogen unable to hydrogen bond F. Anomeric carbon CH3 OH 'N' O-P-o-P-o OH OH он он но OH G. A structure able to participate in T- T stacking

Biology (MindTap Course List)

11th Edition

ISBN:9781337392938

Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Publisher:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg

Chapter3: The Chemistry Of Life: Organic Compounds

Section: Chapter Questions

Problem 4TYU: The synthetic process by which monomers are covalently linked is (a) hydrolysis (b) isomerization...

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Column A shows the names of some of the important functional groups. Column B shows their structures. Match each entry in column A with one in column B
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You are studying a catalytic protein which contains two ion clusters, one cluster contains 2 Cu+3 cations, while the second contains 4 SO3-2 anions. One cluster is held in place deep in the active site of the protein, while the second is near the surface of the protein and involved in regulating the enzyme. Explain how each of the secondary structure elements could bind to these ions, include the region of the secondary structure element or the amino acids involved in this binding.
3.2
1. What will happen if there is a change in the configuration of a protein molecule? Provide an example. 2. Give the IUPAC name for Ala-Gly-Leu
I try to prepare for my biological chemistry exam, so I will appreciate if the answer is with some details. And I will be happy if there would be explanation for when I should use wich of the pka's. Thank you so much.
1. a. Draw the following pentapeptide: lysine-leucine-aspartate-threonine-phenylalanine b. Label the amino and carboxyl terminus of your peptide c. Label each amino acid residue with one and three letter abbreviations d. Label the alpha carbons e. Label the bonds around which phi and psi rotational angles occur f. Which amino acid in this chain is most likely to be phosphorylated? Which amino acid is most likely to be acetylated?
Help me please...
fill in all lettered spaces
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