Biology: Life on Earth with Physiology (11th Edition)
11th Edition
ISBN: 9780133923001
Author: Gerald Audesirk, Teresa Audesirk, Bruce E. Byers
Publisher: PEARSON
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Chapter 3.4, Problem 1CSC
Infectious prions such as those that cause mad cow disease are abnormally folded versions of a protein that is found throughout the body. The secondary structure of the normal prion protein is primarily helical. Infectious prions, however, fold into pleated sheets. The pleated sheets are so stable they are unaffected by the enzymes that break down normal prion protein. As a result, infectious prions accumulate destructively in the brain.
Helices and pleated sheets are the two major secondary structures of proteins. What do protein tertiary and Quaternary structures look like?
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The structure of an alpha helix orients the oxygens of the carbonyl group of the peptide bond towards the C-terminal end of the helix while the hydrogens of the NH groups orient toward the N-terminal end, thus imparting a dipole along the length of the helix. As a result, which kinds of amino acids would favor the C-terminal end, and which would favor the N-terminal end?
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A M A K K E S H I F T A I D E
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Chapter 3 Solutions
Biology: Life on Earth with Physiology (11th Edition)
Ch. 3.1 - define organic molecules and explain why carbon is...Ch. 3.1 - which of these is/are polar molecules? (you may...Ch. 3.1 - explain why functional groups are important in...Ch. 3.1 - name and describe the properties of seven...Ch. 3.2 - define organic molecules and explain why carbon is...Ch. 3.3 - describe the major types of carbohydrates?Ch. 3.3 - A 19-year old 6' 2' male weighing 297 pounds comes...Ch. 3.3 - Describe hydrolysis of this molecule.Ch. 3.3 - provide examples of each type of carbohydrate and...Ch. 3.4 - Infectious prions such as those that cause mad cow...
Ch. 3.4 - describe protein subunits and how proteins are...Ch. 3.4 - Look up the rest of the amino acids and. based on...Ch. 3.4 - explain the four levels of protein structure and...Ch. 3.4 - Why do many proteins, when heated excessively....Ch. 3.4 - list several functions of proteins and provide...Ch. 3.4 - describe the properties of Intrinsically...Ch. 3.5 - Puzzling Proteins All cells use DNA as a blueprint...Ch. 3.5 - describe the general structure of nucleotides?Ch. 3.5 - Why a Perm Is (Temporarily) Permanent?Ch. 3.5 - list three different functions of nucleotides?Ch. 3.5 - explain how nucleic acids are synthesized?Ch. 3.5 - give two examples of nucleic acids and their...Ch. 3.6 - Prob. 1CSRCh. 3.6 - FIGURE 3-22 Synthesis of a triglyceride...Ch. 3.6 - compare and contrast the structure and synthesis...Ch. 3.6 - An obese 55-year-old woman consults her physician...Ch. 3.6 - What kind of reaction breaks this molecule apart?Ch. 3.6 - why are steroid hormones able to diffuse through...Ch. 3.6 - describe the functions of fats, oils, and waxes?Ch. 3.6 - Why are steroid hormones able to diffuse through...Ch. 3.6 - Prob. 3CYLCh. 3 - Based on their structure, sketch and explain how...Ch. 3 - In organic molecules made of chains of subunits,...Ch. 3 - Polar molecules a. dissolve in lipids. b. are...Ch. 3 - Prob. 1RQCh. 3 - Prob. 2ACCh. 3 - Prob. 2FIBCh. 3 - Prob. 2MCCh. 3 - List the four principal classes of biological...Ch. 3 - Prob. 3ACCh. 3 - Prob. 3FIBCh. 3 - Prob. 3MCCh. 3 - Prob. 3RQCh. 3 - Prob. 4FIBCh. 3 - Which of the following is not composed of...Ch. 3 - Prob. 4RQCh. 3 - Fill in the following with the appropriate type of...Ch. 3 - Prob. 5MCCh. 3 - Prob. 5RQCh. 3 - Describe the synthesis of a protein from amino...Ch. 3 - Where in nature do we find cellulose? Where do we...
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- Which of the following statements are true? The local folding of the polypeptide in some regions gives rise to the secondary structure of the protein. The most common secondary structures are the α-helix and β-pleated sheet structures. Certain amino acids have a propensity to form an α-helix, while others have a propensity to form a β-pleated sheet. Select the correct answer below: 1 and 2 1 and 3 2 and 3 all of the abovearrow_forwardAlpha-helices have 3.6 amino acid residues per turn, ie a helix 36 amino acids long would form 10 turns, and The axial distance between adjacent residues is 3.5 Angstroms. Beta-helices have two residues per repeat unit which gives the beta-strand a 7 Angstrom pitch. This compares with the alpha-helix where the axial distance between adjacent residues is only 1.5 Angstroms. Then how many residues in an alpha-helix conformation would it take to traverse the same distance as 10 residues in beta-strand conformation?arrow_forwardA protein in its native three dimensional conformation is cleaved with trypsin. According to the amino acid sequence, there are 9 residues where trypsin could cleave, yet only 3 fragments were produced from the digest. What conclusion can be made about protein structure that would lead to this result? The protein has multiple domains b. The protein is highly compacted, minimally accessible by solvent molecules c. The protein has quaternary structure d. The protein has a dynamic structure, highly accessible by solvent molecules e. The protein is compromised only of alpha helicesarrow_forward
- What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.arrow_forwardConsider 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?arrow_forwardWhich of the following statements are true? Electrostatic interactions are the dominant forces in protein molecular recognition. When two proteins form a complex there is an unfavorable loss of rotational-translational entropy. Protein-protein interfaces are most often dry. The exclusion of water results in an unfavorable loss in rotational-translational entropy. The free energy change associated with the formation of an enzyme-substrate complex almost always results in an unfavorable reduction in conformational entropy of the proteins. Burial of an uncompensated positive charge inside proteins is usually unfavorable. So-called van der Waals’ interactions are essentially electrostatic in origin. Steric complementarity of the two partners forming a complex is essential to achieve optimal free energy of binding. Structural models of proteins obtained from low temperature crystallography are excellent descriptions of all biochemically relevant aspects of their function.arrow_forward
- Refer to the figure below. Replacing lysine with another amino acid in the protein may alter the shape and function of the protein. Replacing lysine with which type(s) of amino acid(s) would lead to the least amount of change in the tertiary structure of this protein? Explain.arrow_forwardGiven that an α helix has 3.6 residues per turn and the rise along the α helix axis is 5.4 Å, approximately how many amino acids would you find in a single contiguous α helix that is 210 Å long?arrow_forwardList some of the possible combinations of α-helices and βsheets in supersecondary structures.arrow_forward
- Consider the following protein sequence as an α helix: Leu-Lys-Arg-Ile-Val-Asp-Ile-Leu-Ser-Arg-Leu-Phe-Lys-Val. how many turns does this helix make?arrow_forwardWhich of the following sequences is most likely to form an unstructured loop in a protein structure? A. GPGGGGGPGGG B. VEELLSKVKQLADA C. KVDFHVNDVEVKMHarrow_forwardProtein 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 rightarrow_forward
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