Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
10th Edition
ISBN: 9780133922851
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 12TYU
WRITE ABOUT A THEME: ORGANIZATION Proteins, which have diverse functions in a cell, are all
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Amino acids are monomers from which proteins are constructed. Understanding the structure and
characteris-tics of amino acids and the peptide bond that covalently links them to form peptides will
aid in understanding larger, more complex protein structures. Proteins carry out a multitude of different
and important functions. The great variety in function is accomplished through a complex and variable
polymeric structure. Comprehending protein structure will give you a better understanding of how proteins
carry out their roles.
Why
Outcomes
1. Use the acid/base characteristics (pK, data) of the 20 amino acids found in proteins to determine the
charge of an amino acid at a given pH.
2. Determine the pI of a small peptide.
3. Identify the peptide bond and describe the structural features that characterize a peptide bond.
4. Use information processing skills to draw conclusions about chemical characteristics of complex
molecules.
Plan
1. Form teams as instructed.
2. The person whose…
Protein structure is directly related to function. Which of the following statements is true regarding this concept ?
Polypeptide backbone
-CH2 – CH, – CH2- CH2- NH3 0-c- CH -
CH2
lonic bond
Hydrogen !
bond
C- NH2
Disulfide
linkage
CH
CH2
HạC
CH3
CH3
H3C
CH
-CH2
Hydrophobic
interactions
A. The primary structure consists of the DNA sequence. The secondary and tertiary structures are dependent on interactions between the DNA and RNA polymerase. Mutations resulting in changes one or
more bases has the potential to destroy the structure, and therefore the function, of the protein.
B. The primary structure consists of the amino acid sequence. The secondary and tertiary structures are dependent on interactions between the amino acid side chains. Mutations resulting in changes one or more
amino acids has the potential to destroy the structure, and therefore the function, of the protein.
C. The primary structure consists of the DNA sequence. The secondary structure consists of the amino acid…
Identify and describe the polymer structures of a protein that constitutes its unique conformation.
(b) Enzymes function is dependent upon its shape. Identify ONE environmental factor and explain the way in which it affects its function.
refer to picture
Chapter 5 Solutions
Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
Ch. 5.1 - What are the four main classes of large biological...Ch. 5.1 - How many molecules of water are needed to...Ch. 5.1 - WHAT IF? If you eat a piece of fish, what...Ch. 5.2 - Write the formula for a monosaccharide that has...Ch. 5.2 - Prob. 2CCCh. 5.2 - WHAT IF? After a cow is given antibiotics to...Ch. 5.3 - Compare the structure of a fat (triglyceride) with...Ch. 5.3 - Why are human sex hormones considered lipids?Ch. 5.3 - Prob. 3CCCh. 5.4 - What parts of a polypeptide participate in the...
Ch. 5.4 - Prob. 2CCCh. 5.4 - WHAT IF? Where would you expect a polypeptide...Ch. 5.5 - Prob. 1CCCh. 5.5 - DRAW IT In a DNA double helix, a region along one...Ch. 5.6 - How would sequencing the entire genome of an...Ch. 5.6 - Given the function of DNA, why would you expect...Ch. 5 - What is the fundamental basis for the differences...Ch. 5 - Compare the composition, structure, and function...Ch. 5 - Why are lipids not considered to be polymers or...Ch. 5 - Explain the basis for the great diversity of...Ch. 5 - What role does complementary base pairing play in...Ch. 5 - Prob. 5.6CRCh. 5 - Prob. 1TYUCh. 5 - The enzyme amylase can break glycosidic linkages...Ch. 5 - Prob. 3TYUCh. 5 - The structural level of a protein least affected...Ch. 5 - Enzymes that break down DNA catalyze the...Ch. 5 - The molecular formula for glucose is C6H12O6. What...Ch. 5 - Which of the following pairs of base sequences...Ch. 5 - Construct a table that organizes the following...Ch. 5 - Prob. 9TYUCh. 5 - EVOLUTION CONNECTION Comparisons of amino acid...Ch. 5 - SCIENTIFIC INQUIRY Suppose you are a research...Ch. 5 - WRITE ABOUT A THEME: ORGANIZATION Proteins, which...Ch. 5 - SYNTHESIZE YOUR KNOWLEDGE Given that the function...
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- Describe the four levels of protein structures. Include information about the bond between amino acids, and for the third level of protein structure, discuss the other types of bond found there. Make sure you include hydrogen bonds, ionic bonds, and an example of covalent bonding. Explain why not all proteins form a quaternary structure.arrow_forwardSelect the true statements about protein secondary structure. In an a-helix, the side chains are located on the outside of the helix. The secondary level of protein structure refers to the spatial arrangements of short segments of the protein. In a B-pleated sheet, the side chains are located between adjacent segments. Peptide bonds stabilize secondary structure. The x-helix is held together by hydrogen bonds between the amide N-H and C=O groups. Incorrectarrow_forwardBiochemists talk about protein structure at four distinct levels: primary, secondary, tertiary and quaternary structure. Below are depictions of each of these levels of protein structure. For each image, match the term and the written description of the level of protein structure that the image depicts. Drag the appropriate items to their respective bins.arrow_forward
- Explain Four Levels of Protein Structure with examples and talk about the importance of each structure (Primary, Secondary, Tertiary, and Quaternary structure). With photos pleasearrow_forwardMatch the protein structure terms on the left with the descriptions on the right. v (Choose ) commonly observed combinations of secondary structural elements tertiary structure Long segments of secondary structure. supersecondary structure basic component of quaternary structure Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the peptide Spatial arrangement of peptide atoms, stabilized by non-covalent interactions between atoms found within the side chain compact structural or functional regions within a given polypeptide functional structures formed by non-covalent interactions between multiple polypeptides. domain (Choosel subunit quaternary structure (Choose)arrow_forwardDiscuss using your own words and illustrations the organisation of a protein, from its linear amino acid sequence, to its final three–dimensional configuration, which may include one or more polypeptides. Include what types of bonds help to stabilise each structural level, from primary through quaternary structure.arrow_forward
- Protein structures have several different levels of organization. In the space below indicate the type of molecular bonds that can contribute to each level of organization: primary- secondary- tertiary- quarternary-arrow_forwardMatch the following levels of protein structure with their description two or more polypeptide chains > > twisting and folding to form a 3-dimensional structure, dependent on the locations of the charged groups and polar groups within the amino acid chain, sometimes covalent bonds form between sulfur atoms (called disulfide bonds) alpha helix and beta- pleated sheets formed by the arrangement of hydrogen bonds between amino acids, many other shapes are possible amino acid sequence 1. quaternary 2. tertiary 3. primary 4. secondaryarrow_forwardWhat life uses proteins for? (functions of proteins) Describe protein structures. Describe the alpha helix and the beta sheet structure of proteins. Which structure is the most important in the function of a protein? Describe what can affect the protein structure. Why the structure of a protein is important?arrow_forward
- Physical methods are often used to determine protein conformation. Describe how x-ray crystallography, cryo electron microscopy, and NMR spectroscopy can be used to determine the shapes of proteins. What are the advantages and disadvantages of each method? Which is better for small proteins? Large proteins? Huge macromolecular assemblies?arrow_forwardGive typing answer with explanation and conclusionarrow_forwardProteins, which have diverse functions and a cell, are all polymers of the same kinds of monomers-amino acids. Describe how the structure of amino acids allow proteins to perform so many functions.arrow_forward
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