Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 31, Problem 12P
Understanding the Nature of the Ubiquitin-Ubiquitin linkage Draw the structure of the isopeptide bond formed between
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Using Fig. as a guide, draw the complete structure of a nucleoside triphosphate before and after it becomes incorporated into a polynucleotide chain. Draw the structure that would result if the newly formed phosphodiester bond were hydrolyzed.
Based from the table draw the structure of tripeptife ILY at ph 7
Choose if it's true or false
Different from RNA since in the latter the internucleotide linkages are between C-2’ and C-5’
A long chain polymer in which the internucleotide linkages are of the diester type between C-3’ and C-5’
Usually present in tissues as a nucleoprotein and cannot be separated from its protein component
Hydrolyzed by weak alkali (pH 9 to 100°C)
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- A synthetic polypeptid made up of L-glutamic acid residues is in a random coil configuration at pH 7.0 but changes to alpha helical when the pH is lowered to 2.0. Explain this pH-dependent conformational transition.arrow_forwardMacmillan Learning The graphs show a titration curve for the amino acid histidine. Label the fist curve with the major histidine species at each position. One histidine species will not be used. Label the second curve with the pKå values for the histidine functional groups and the isoelectric point (pI) of histidine. 14 12 10 8 HH pH 6 His [His] = [His] 2 His²- [His² +] = [His*] 0 0.0 0.5 1.0 Incorrect Answer 1.5 [OH-] (equivalents) Hisº His [His] = [His] 2.0 2.5 3.0 His² + Answer Bankarrow_forwardNeed help The β chains of HbA and HbS were treated with trypsin, and the sequence of the N-terminal tryptic peptides are as given below. Do these peptides separate from each other in an electric field if the pH is 7.0? Explain in detail the reasoning behind your answer and include your calculations for the charge of each peptide in your answer. HbA: Val-His-Leu-Thr-Pro-Glu-Glu-Lys HbS: Val-His-Leu-Thrarrow_forward
- Ala-Arg-Val-His-Asp-Gln Given the polypeptide chain above Estimate the net charge of the polypeptide chain at physiological pH (7.4) and at pH 5.0 . How many peptide bonds are there? What kind of polypeptide is it?arrow_forwardi. A schematic structure of the subunit of hemerythrin (an oxygen-binding protein from invertebrate animals) is shown to the right. (a) It has been found that in some of the a-helical regions of hemerythrin, about every third or fourth amino acid residue is a hydrophobic one. Suggest a structural reason for this finding. (b) What would be the effect of a mutation that placed a proline residue at point A in the structure?arrow_forwardUnderstanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.arrow_forward
- Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet point alternately above and below the plane of the sheet, consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg- Leu-Lys-Ile-Arg-Phe-Glu. Do you find anything remarkable about the arrangement of the amino acids in this sequence when incorporated into a β sheet? Can you make any predictions as to how the β sheet might be arranged in a protein?arrow_forwardLet's consider a protein with two surface-exposed histidine residues: • Hisa is a "typical" histidine residue with pKa = 6.2 Hisg is involved in a stabilizing interaction (His-NH* --- -02C-Glu) with a neighboring glutamic acid residue. For Hisg, the Gibbs free energy of deprotonation at pH = 7.0 and T = 293 K is AG'° = +15 kJ mol-1. If you had a solution, at pH = 7.0 and T = 293 K, containing this protein: a) What fraction of Hisa residues are protonated? b) What fraction of Hisg residues are protonated? c) What is the pK, of Hisg?arrow_forwardA. Write the structure of the following peptide at pH 5.0 and calculate its net charge at this pH. Asp-His-Tyr-Arg-Lys-Leu-Thr-Gln. Based on the pKa value of the ionizable groups. B. A polypeptide consisting only of L-glutamate residues (poly-L-glutamate) may have a random coil or helical structure depending on pH. Explain this behavior by indicating at what pH values the helical structure will be favored.arrow_forward
- Figure 1 shows the structure of adenine and thymine. (i) (ii) NH adenine C-H thymine Figure 1 Illustrate the potential tautomers of adenine and thymine. Draw a chemical structure of Thyminc-Adenine (T-A) base pair and label the patterns of hydrogen bond acceptors, donors in the major groove of the TA base pair.arrow_forwardLoop regions play important roles in the secondary structure of protein. Define loop region and give three (3) of the rolesarrow_forwardGiven: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?arrow_forward
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