EBK HUMAN PHYSIOLOGY
8th Edition
ISBN: 9780134704227
Author: Silverthorn
Publisher: YUZU
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Textbook Question
Chapter 4, Problem 23RQ
On what molecule does the anticodon appear? Explain the role of this molecule in protein synthesis.
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Consider the following peptide to answer the questions below:
A M A K K E S H I F T A I D E
What is the total charge of this peptide at pH = 5?
What is the N terminal amino acid (full name)? C terminal amino acid?
How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)?
Would this peptide be a candidate to form an alpha helix? Why or why not
Consider the following in light of the concept of levels of structure (primary, secondary, tertiary, quaternary) as defined for proteins. (a) What level is shown by doublestranded DNA? (b) What level is shown by tRNA? (c) What level is shown by mRNA?
What are the two main steps to protein synthesis and where do they take place?
What are the different types of RNA used and what are their roles?
How important is nucleotide order to the process?
Chapter 4 Solutions
EBK HUMAN PHYSIOLOGY
Ch. 4.1 - Which biomolecules always include nitrogen in...Ch. 4.1 - Prob. 2CCCh. 4.1 - What is the difference between potential energy...Ch. 4.1 - Prob. 4CCCh. 4.2 - Prob. 5CCCh. 4.2 - Prob. 6CCCh. 4.2 - Prob. 7CCCh. 4.3 - Prob. 8CCCh. 4.3 - Prob. 9CCCh. 4.3 - Prob. 10CC
Ch. 4.3 - Prob. 11CCCh. 4.4 - Name five ways in which cells regulate the...Ch. 4.4 - Prob. 13CCCh. 4.4 - Prob. 14CCCh. 4.4 - Match each component on the left to the...Ch. 4.4 - Prob. 16CCCh. 4.4 - How is the separation of mitochondria into two...Ch. 4.4 - Prob. 18CCCh. 4.4 - Prob. 19CCCh. 4.4 - Prob. 20CCCh. 4.4 - What does the name RNA polymerase tell you about...Ch. 4.4 - Explain in one or two sentences the relationship...Ch. 4.4 - Prob. 23CCCh. 4.4 - List three general types of posttranslational...Ch. 4.4 - Prob. 25CCCh. 4 - List the three basic forms of work and give a...Ch. 4 - Prob. 2RQCh. 4 - Prob. 3RQCh. 4 - Prob. 4RQCh. 4 - Prob. 5RQCh. 4 - Prob. 6RQCh. 4 - Match each definition in the left column with the...Ch. 4 - Prob. 8RQCh. 4 - Organic molecules that must be present in order...Ch. 4 - In an oxidation-reduction reaction, in which...Ch. 4 - Prob. 11RQCh. 4 - Prob. 12RQCh. 4 - Prob. 13RQCh. 4 - Metabolic regulation in which the last product of...Ch. 4 - Prob. 15RQCh. 4 - Prob. 16RQCh. 4 - Create maps using the following terms.Ch. 4 - Prob. 18RQCh. 4 - Prob. 19RQCh. 4 - Prob. 20RQCh. 4 - Prob. 21RQCh. 4 - Briefly describe the processes of transcription...Ch. 4 - On what molecule does the anticodon appear?...Ch. 4 - Is the energy of ATPs phosphate bond an example of...Ch. 4 - Prob. 25RQCh. 4 - Prob. 26RQCh. 4 - Prob. 27RQCh. 4 - Prob. 28RQ
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- How does the process of protein synthesis differ in Prokaryotes and Eukaryotes? Discuss factors other than ribosome size.arrow_forwardShown below are two cartoon views of the small globular protein StrepG inwhich an α helix is packed against a four-strand β sheet. The sheet is madeup of two “β-hairpins” (a β-hairpin is a “β-turn-β” structure). Refer to theimages and answer the questions that follow: (a) Identify the locations of the N- and C-termini of StrepG.(b) Indicate the orientation of the helical macrodipole, showing the (δ+)and (δ-) ends of the macrodipole.(c) How many residues are in the helix?(d) Do you predict that the α helix and β sheet are amphiphilic or not?Briefly explain.(e) The following two peptides are part of the primary sequence of StrepG.Based on your answer to part (d), which one is more likely to correspondto the α helix? Which is most likely to be part of a β-hairpin? Explainyour choice.Peptide #1: DAATAEKVFKQYAND or Peptide #2: VDGEWTYDDATKTFTVarrow_forwardCan the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.arrow_forward
- A monomeric protein contains 154 amino acids. How many codons code for these amino acids? How many nucleotides?arrow_forward1) What are the four levels of protein folding. How do you distinguish those different levels? What can denature a protein? 2) What are detergents and why are they useful? How do they basically work? 3) What is meant by amphipathic? What is an example of this?arrow_forwardWhy is carboxyl terminal domain (CTD) phosphorylation functionally important?arrow_forward
- What forces come into play with protein folding (please explain this at the molecular level)?arrow_forwardRibosomes Are the Sitesof Polypeptide Synthesis EXPLAIN HOW?arrow_forwardAmino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?arrow_forward
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Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY