Campbell Biology: Concepts & Connections, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (8th Edition)
8th Edition
ISBN: 9780133909029
Author: Jane B. Reece, Martha R. Taylor, Eric J. Simon, Jean L. Dickey, Kelly A. Hogan
Publisher: PEARSON
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Chapter 3, Problem 14TYK
How can a cell make many different kinds of proteins out of only 20 amino acids? Of the myriad possibilities, how does the cell “know” which proteins to make?
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What is the concepts of the native conformation of proteins? Why and how do proteins refold and unfold?
Shown below is an internal fragment of a polypeptide. If this polypeptide were growing, onto which end would the next amino acid be added?
a) Onto the right
b) Onto the left
Shown below is an internal fragment of a polypeptide. If this polypeptide were growing, onto which end would the next amino acid be added?
a) onto the right
b) onto the left
Chapter 3 Solutions
Campbell Biology: Concepts & Connections, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (8th Edition)
Ch. 3 - Complete the following table to help you review...Ch. 3 - A glucose molecule is to starch as (Explain your...Ch. 3 - What makes a fatty acid an acid? a. It does not...Ch. 3 - Prob. 4TYKCh. 3 - Of the following functional groups, which is/are...Ch. 3 - Prob. 6TYKCh. 3 - Prob. 7TYKCh. 3 - Prob. 8TYKCh. 3 - Which structural level of a protein would be least...Ch. 3 - Circle and name the functional groups in this...
Ch. 3 - Most proteins are soluble in the aqueous...Ch. 3 - Sucrose is broken down in your intestine to the...Ch. 3 - The diversity of life is staggering. Yet the...Ch. 3 - How can a cell make many different kinds of...Ch. 3 - Given that the function of egg yolk is to nourish...Ch. 3 - Enzymes usually function best at an optimal pH and...Ch. 3 - SCIENTIFIC THINKING Another aspect of the Nurses...
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- HOW MANY DIFFERENT PROTEINS CAN BE CONSTRUCTED THAT ARE EXACTLY FOUR AMINO ACIDS LONG? (HINT: THERE ARE 20 POSSIBLE AMINO ACIDS.)arrow_forwardWhy are multifunctional proteins necessary and/ordesirable?arrow_forwardoligosaccharides are attached to proteins for a variety of reasons. They’re attached to the newly synthesized proteins in the endoplasmic reticulum and golgi apparatus to assign them destination labels, misfolded protein labels, and quality control labels. How does the polarity and charge of these oligosaccharides affect the protein they are bound to?arrow_forward
- Consider the peptide in the image and answer the following questions.arrow_forwardwhat are the four levels of protein structure? what stabilizes each level of folding? what environmental factors affect protein folding?arrow_forwardThe proteins in an organism’s cells are diverse (in number) and complex (in structure and function). How is this so when there are only 20 amino acids that would make them?arrow_forward
- Why do you suppose only l-amino acids and not a random mixture of the l- and d-forms of each amino acid are used to make proteins?arrow_forwardIn the figure below, protein 1 is located in the cytosol, and protein 2 is membrane bound. Give 3 specific examples from Figure 4-3 of amino acids that you might expect to find on the surface of protein 1. For protein 2, give three specific amino acids that you would expect to be on the surface near both points A and B (labeled with stars). To clarify, you should choose 3 amino acids for point A and also list three amino acids for point B. All of the amino acids you choose for Protein 2 must be different from those that you choose for Protein 1. Rationalize your choices by discussing the amino acids you chose, and their properties in a few sentences. Protein 1 Protein 2arrow_forwardRose loves eating oats for her breakfast. Her friend Lisa who is a chemist, found out that oats contain 0.11 mole arginine, 0.5 histidine and 0.4 lysine. What is the % of arginine in the protein present in oats? Unknown: Given: Formula: Solution: Final Answer:arrow_forward
- Describe the following levels of protein organization and give an example of each: A.) Primary B.) Secondary C.) Tertiary D.) Quarternaryarrow_forwardHow many different types of protein-protein interfaces are found in a tetrahedral cage, octahedral cage, and icosahedral cage, respectively?arrow_forward* hat do you think holds together the various secondary structural elements in a Particular three-dimensional pattern? (Hint: Look back at Figure 4 - what is sticking out from the sides of the a-helices and B-strands?) glutamic acid B CH, CH valine CH H-N CH H. valine alanine CH2 CH2 lysine Figure 4-4 Essential Cell Biology 3/e (O Garland Science 2010) Figure 6. Three examples of bonding interactions that stabilize the tertiary structures of proteins (indicated by arrows A, B,and C). Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission Garland Science/ Taylor & Francis LLC. CH2 CH, SH SH CH2 CH2 OXIDATION CH2 SH REDUCTION SH CH2 CH2 Figure 4-26 Essential Cell Bialogy 3e o Garland Science 2010) Figure 7. Disulfide bonds within proteins can form (left-pointing arrow) or be broken (right- pointing arrow), depending on their chemical surroundings (oxidative or reducing). Copyright 2013 from Essential Cell Biology,4th Edition by Alberts et al.…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