Human Physiology
15th Edition
ISBN: 9781259864629
Author: Fox, Stuart Ira
Publisher: Mcgraw-hill Education,
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Chapter 2, Problem 22RA
Summary Introduction
To review:
The relation between tertiary, secondary, and primary structures of proteins, and changes in tertiarty protein structure due to alteration in the nature of amino acids in the primary structure of protein.
Introduction:
The proteins are macromolecules having polypeptide chains of 20 different amino acids. Proteins play different roles at different sites such as some act as catalytic enzymes in various biological reactions, or as hormones and membrane receptors in cells.
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Identify the following statements as descriptive of the secondary, tertiary, or quaternary structure of a protein. What types of interactions stabilize each type of structure?(a) The polypeptide chain has a number of bends and twists, resulting in a compact structure.(b) The polypeptide backbone forms a right-handed coil.(c) The four polypeptide chains are arranged in a spherical shape.
Protein folding is critical for function because the properties of a protein arise from its overall shape and the distribution within that shape of the various amino acid side-chains. Which of the following statements about protein three-dimensional structure are correct?
1) the folding pattern of a protein is ultimately determined by its amino acid sequence.
2) proteins tend to fold in such a way that the hydrophobic amino acids are buried in the interior, while hydrophilic amino acids are exposed at the surface.
3) the chemical interactions within a protein molecule that support its overall folded structure are mostly covalent C-C (carbon to carbon) bonds between amino acid side-chains.
4) the overall folding pattern/shape of a protein molecule is termed its primary structure.
5) during evolution, the three-dimensional structure of a protein is often more strongly conserved than its amino acid sequence.
More than one answer might be right
Together, these monomers make up what type of polymer (macromolecule)?
List at least three (broad) functions that these macromolecules can perform. What is an example protein that we’ve discussed that uses of these functions?
Using R as the side chain, draw the basic structure of an amino acid.
Chapter 2 Solutions
Human Physiology
Ch. 2 - List the components of an atom and explain how...Ch. 2 - Describe the nature of nonpolar and polar covalent...Ch. 2 - Define the terms acidic, basic, acid, and base....Ch. 2 - Using chemical equations, explain how bicarbonate...Ch. 2 - Prob. 4CPCh. 2 - Describe the structural characteristic of all...Ch. 2 - Describe the characteristics of a lipid, and...Ch. 2 - Explain, in terms of dehydration synthesis and...Ch. 2 - Relate the functions of phospholipids to their...Ch. 2 - Write the general formula for an amino acid, and...
Ch. 2 - Describe and account for the different levels of...Ch. 2 - Describe the different categories of protein...Ch. 2 - Prob. 10aCPCh. 2 - Prob. 10bCPCh. 2 - Describe the structure of DNA, and explain the law...Ch. 2 - Which of these statements about atoms is true?...Ch. 2 - The bond between oxygen and hydrogen in a water...Ch. 2 - Which of these is a nonpolar covalent bond?...Ch. 2 - Solution A has a pH of 2, and solution B has a pH...Ch. 2 - Glucose is
Ch. 2 - Digestion reactions occur by means of...Ch. 2 - Carbohydrates are stored in the liver and muscles...Ch. 2 - Lecithin is
Ch. 2 - Which of these Lipids have regulatory roles in the...Ch. 2 - The tertiary structure of a protein is directly...Ch. 2 - The type of bond formed between two molecules of...Ch. 2 - The carbon-to-nitrogen bond that joins amino acids...Ch. 2 - Prob. 13RACh. 2 - Prob. 14RACh. 2 - Prob. 15RACh. 2 - Prob. 16RACh. 2 - Prob. 17RACh. 2 - Explain, in terms of dehydration synthesis and...Ch. 2 - Prob. 19RACh. 2 - Prob. 20RACh. 2 - Explain how one DNA molecule serves as a template...Ch. 2 - Prob. 22RACh. 2 - Prob. 23RACh. 2 - From the ingredients listed on a food wrapper, it...Ch. 2 - Prob. 25RACh. 2 - Prob. 26RACh. 2 - Prob. 27RACh. 2 - Prob. 28RACh. 2 - Prob. 29RACh. 2 - The molecular weight is the sum of the atomic...
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- How do the following interactions help to stabilize the tertiary and quaternary structure of a protein? Give an example of a pair of amino acids that could give rise to each interaction.(a) Side-chain hydrogen bonding(b) Disulfide bondsarrow_forwardDiscuss and identify the four levels of protein structure (primary, secondary, tertiary,and quaternary). Explain how the structure of a protein affects its properties and howdenaturation changes the structure.arrow_forwardWhat primarily determines the secondary and tertiary structures of a protein?arrow_forward
- Which of the following amino acids is most likely to be found on the outside of a soluble protein, and which of them is more likely to be found on the inside? Explain each answer. (Hint: Consider the effect of the amino acidside chain in each case and that the protein is folded up into its globular form.)(a) Valine (b) Aspartate(c) Histidine (d) Alaninearrow_forwardName and discuss the non-covalent interactions that maintain protein structure. Explain the chirality of amino acid molecules.arrow_forwardDescribe as completely as possible, the four levels of protein What type of bonds hold a protein together at the primary level? What type of bonds maintain the protein at the secondary and tertiary level? Give an example of secondary, tertiary, and quarternary level proteins. At which level is the protein functional? What happens (at a molecular level) when a protein is denatured?arrow_forward
- A) List each of the five major functional classes of proteins. B) Discuss the function for each class, give an example of a protein for each class and mention how the function of the protein example fits the function of the class (40 words or less for each class with its examplearrow_forwardDo physical and chemical conditions affect the structure of a protein?arrow_forwardGlycine provides structural flexibility in proteins. What is the consequence of this on protein structure?arrow_forward
- what are the four interactions that keep the protein structure intact?arrow_forwardDraw the chemical structure of an alanine pentapeptide. Indicate the location of each peptide bond. Label the phi () and psi () dihedral angles. Name and briefly define the four levels of protein structure.arrow_forwardWhat level of protein structure is determined by the following:(a) Peptide bonds between amino acids?(b) Hydrogen bonds between backbone carbonyl oxygen atoms and hydrogen atoms attached to backbone nitrogen atoms?(c) R group interactions that may involve Van der Waalsforces, ionic interactions, or hydrogen bonds?arrow_forward
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