General, Organic, And Biological Chemistry, Hybrid (with Owlv2 Quick Prep For General Chemistry Printed Access Card)
7th Edition
ISBN: 9781305253070
Author: STOKER, H. Stephen
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 20, Problem 20.97EP
Indicate whether each of the following statements concerning secondary protein structure is true or false.
- a. Hydrogen bonds present in an α helix structure involve two adjacent amino acids.
- b. Both α helix and β pleated sheet structures can be present in the same protein.
- c. In a β pleated sheet structure, the hydrogen bonding is always between different protein chains.
- d. In an α helix, all of the amino acid R groups lie inside the helix.
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
Which of the following statements are correct about protein structure (select all that apply)?
A.
Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein
B.
Only amino acids with a net charge may interact with other amino acids
C.
The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role.
D.
Hydrophobic interactions play a key role in protein folding
E.
Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acids
Which of the following statement about proteins is correct
a. alpha helix and Beta pleated sheets are considered quaternary structures
b. a single polypeptide only has primary sytructure, secondary, tertiary, and quaternary structures require more than one polypeptide
c. there are 30 essential amino acids that are the monomer building blocks of proteins
d. polypeptides have a distinct polarity (directionality) with one end refered to as the free amino end, and the other called the free carboxyl end
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are:
a. always side by side.
b. generally near each other in sequence.
c. invariably restricted to about 7 of the 20 standard amino acids.
d. often on different polypeptide strands.
e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
Chapter 20 Solutions
General, Organic, And Biological Chemistry, Hybrid (with Owlv2 Quick Prep For General Chemistry Printed Access Card)
Ch. 20.1 - Prob. 1QQCh. 20.1 - Proteins are naturally occurring unbranched...Ch. 20.2 - Prob. 1QQCh. 20.2 - How do the various standard amino acids differ...Ch. 20.2 - The number of carboxyl groups and amino groups...Ch. 20.2 - How many different subclassifications are there...Ch. 20.2 - Which of the following statements concerning...Ch. 20.3 - Prob. 1QQCh. 20.3 - Proteins from plant sources are a. always complete...Ch. 20.3 - Prob. 3QQ
Ch. 20.4 - Prob. 1QQCh. 20.4 - Which of the following groups is positioned at the...Ch. 20.4 - Which of the following statements concerning...Ch. 20.5 - Which of the standard amino acids exist as...Ch. 20.5 - Which of the following is the zwitterion ion...Ch. 20.5 - Which of the following is the structural form for...Ch. 20.6 - Prob. 1QQCh. 20.6 - Prob. 2QQCh. 20.7 - The joining together of two amino acids to form a...Ch. 20.7 - The number of peptide bonds present in a...Ch. 20.7 - Which of the following statements concerning the...Ch. 20.7 - Prob. 4QQCh. 20.7 - How many isomeric tripeptides can be formed from...Ch. 20.8 - The two best-known peptide hormones present in the...Ch. 20.8 - Which of the following peptides is an important...Ch. 20.9 - The term protein is generally reserved for...Ch. 20.9 - Prob. 2QQCh. 20.9 - Which of the following is not a distinguishing...Ch. 20.10 - Specifying the primary structure of a protein...Ch. 20.10 - Prob. 2QQCh. 20.10 - Prob. 3QQCh. 20.11 - Prob. 1QQCh. 20.11 - Prob. 2QQCh. 20.11 - Prob. 3QQCh. 20.12 - Prob. 1QQCh. 20.12 - Hydrophobic interactions associated with protein...Ch. 20.12 - R group interactions between which of the...Ch. 20.13 - Prob. 1QQCh. 20.13 - Which of the following types of interactions does...Ch. 20.14 - The complete hydrolysis of a protein produces a...Ch. 20.14 - Which of the following statements concerning...Ch. 20.15 - Which of the following levels of protein structure...Ch. 20.15 - Which of the following does not involve protein...Ch. 20.15 - Prob. 3QQCh. 20.16 - Prob. 1QQCh. 20.16 - Prob. 2QQCh. 20.16 - Prob. 3QQCh. 20.16 - In which of the following pairs of proteins are...Ch. 20.17 - Insulin and human growth hormone are examples of...Ch. 20.17 - Myoglobin and transferrin are examples of a....Ch. 20.17 - Prob. 3QQCh. 20.18 - Prob. 1QQCh. 20.18 - Prob. 2QQCh. 20.18 - Prob. 3QQCh. 20.19 - Prob. 1QQCh. 20.19 - Which of the following types of plasma...Ch. 20.19 - Prob. 3QQCh. 20 - Prob. 20.1EPCh. 20 - What element is always present in proteins that is...Ch. 20 - What percent of a cells overall mass is accounted...Ch. 20 - Approximately how many different proteins are...Ch. 20 - What is signified when an amino acid is designated...Ch. 20 - What functional groups are present in all -amino...Ch. 20 - Indicate whether or not each of the following...Ch. 20 - Indicate whether or not each of the following...Ch. 20 - How many carbon atoms are present in the R group...Ch. 20 - How many carbon atoms are present in the R group...Ch. 20 - With the help of Table 20-1, determine the name...Ch. 20 - With the help of Table 20-1, determine the name...Ch. 20 - With the help of Table 20-1, classify each of the...Ch. 20 - With the help of Table 20-1, classify each of the...Ch. 20 - Prob. 20.15EPCh. 20 - With the help of Table 20-1, classify each of the...Ch. 20 - Prob. 20.17EPCh. 20 - Prob. 20.18EPCh. 20 - Prob. 20.19EPCh. 20 - Prob. 20.20EPCh. 20 - Prob. 20.21EPCh. 20 - How many amino groups and how many carboxyl groups...Ch. 20 - Prob. 20.23EPCh. 20 - Which two of the standard amino acids are...Ch. 20 - Prob. 20.25EPCh. 20 - Prob. 20.26EPCh. 20 - Prob. 20.27EPCh. 20 - Prob. 20.28EPCh. 20 - Prob. 20.29EPCh. 20 - Prob. 20.30EPCh. 20 - Indicate whether or not the designation...Ch. 20 - Indicate whether or not the designation...Ch. 20 - Prob. 20.33EPCh. 20 - Prob. 20.34EPCh. 20 - To which family of mirror-image isomers do nearly...Ch. 20 - In what way is the structure of glycine different...Ch. 20 - Draw Fischer projection formulas for the following...Ch. 20 - Draw Fischer projection formulas for the following...Ch. 20 - Answer the following questions about the amino...Ch. 20 - Answer the following questions about the amino...Ch. 20 - At room temperature, amino acids are solids with...Ch. 20 - At room temperature, most amino acids are not very...Ch. 20 - Prob. 20.43EPCh. 20 - Draw the zwitterion structure for each of the...Ch. 20 - Draw the structure of serine at each of the...Ch. 20 - Prob. 20.46EPCh. 20 - Prob. 20.47EPCh. 20 - Most amino acids have isoelectric points between...Ch. 20 - Glutamic acid exists in two low-pH forms instead...Ch. 20 - Arginine exists in two high-pH forms instead of...Ch. 20 - In a low-pH aqueous solution, indicate whether...Ch. 20 - Prob. 20.52EPCh. 20 - When two cysteine molecules dimerize, what happens...Ch. 20 - What chemical reaction involving the cysteine...Ch. 20 - What two functional groups are involved in the...Ch. 20 - Write a generalized structural representation for...Ch. 20 - For the tripeptide GlyAlaCys a. What amino acid is...Ch. 20 - For the tripeptide SerValMet a. What amino acid is...Ch. 20 - Prob. 20.59EPCh. 20 - Prob. 20.60EPCh. 20 - Draw a complete condensed structural...Ch. 20 - Draw a complete condensed structural...Ch. 20 - With the help of Table 20-1, identify the amino...Ch. 20 - With the help of Table 20-1, identify the amino...Ch. 20 - With the help of Table 20-1, assign an IUPAC name...Ch. 20 - With the help of Table 20-1, assign an IUPAC name...Ch. 20 - Prob. 20.67EPCh. 20 - Prob. 20.68EPCh. 20 - For the tripeptide AlaValGly which amino acid...Ch. 20 - For the tripeptide SerArgIle which amino acid...Ch. 20 - Consider the tripeptide tyrosylleucylisoleucine....Ch. 20 - Consider the tripeptide leucylvalyltryptophan. a....Ch. 20 - Explain why the notations SerCys and CysSer...Ch. 20 - Explain why the notations AlaGlyValAla and...Ch. 20 - Prob. 20.75EPCh. 20 - There are a total of six different amino acid...Ch. 20 - Compare the structures of the protein hormones...Ch. 20 - Compare the protein hormones oxytocin and...Ch. 20 - Compare the binding-site locations in the brain...Ch. 20 - Compare the structures of the peptide...Ch. 20 - Prob. 20.81EPCh. 20 - Prob. 20.82EPCh. 20 - What is the major difference between a monomeric...Ch. 20 - What is the major difference between a simple...Ch. 20 - Prob. 20.85EPCh. 20 - Prob. 20.86EPCh. 20 - Prob. 20.87EPCh. 20 - Two proteins with the same amino acid composition...Ch. 20 - How many different primary structures are possible...Ch. 20 - How many different primary structures are possible...Ch. 20 - How many different primary structures are possible...Ch. 20 - How many different primary structures are possible...Ch. 20 - Prob. 20.93EPCh. 20 - Draw a segment of the backbone of a protein that...Ch. 20 - Prob. 20.95EPCh. 20 - In a pleated sheet secondary structure for a...Ch. 20 - Indicate whether each of the following statements...Ch. 20 - Indicate whether each of the following statements...Ch. 20 - Prob. 20.99EPCh. 20 - Prob. 20.100EPCh. 20 - State the four types of attractive forces that...Ch. 20 - Prob. 20.102EPCh. 20 - Prob. 20.103EPCh. 20 - Prob. 20.104EPCh. 20 - Prob. 20.105EPCh. 20 - Prob. 20.106EPCh. 20 - Prob. 20.107EPCh. 20 - Prob. 20.108EPCh. 20 - Prob. 20.109EPCh. 20 - Not all proteins have quaternary structure....Ch. 20 - Prob. 20.111EPCh. 20 - Prob. 20.112EPCh. 20 - Prob. 20.113EPCh. 20 - Prob. 20.114EPCh. 20 - Prob. 20.115EPCh. 20 - Prob. 20.116EPCh. 20 - Prob. 20.117EPCh. 20 - Prob. 20.118EPCh. 20 - Identify the primary structure of a hexapeptide...Ch. 20 - Identify the primary structure of a hexapeptide...Ch. 20 - Draw structural formulas for the products obtained...Ch. 20 - Prob. 20.122EPCh. 20 - Which structural levels of a protein are affected...Ch. 20 - Prob. 20.124EPCh. 20 - In what way is the protein in a cooked egg the...Ch. 20 - Why is cooked protein more easily digested than...Ch. 20 - Indicate whether or not each of the following...Ch. 20 - Prob. 20.128EPCh. 20 - Prob. 20.129EPCh. 20 - Contrast fibrous and globular proteins in terms of...Ch. 20 - Classify each of the following proteins as a...Ch. 20 - What is the major biochemical function of each of...Ch. 20 - Prob. 20.133EPCh. 20 - Prob. 20.134EPCh. 20 - Prob. 20.135EPCh. 20 - Prob. 20.136EPCh. 20 - Prob. 20.137EPCh. 20 - Where are the carbohydrate units located in...Ch. 20 - Prob. 20.139EPCh. 20 - Prob. 20.140EPCh. 20 - Prob. 20.141EPCh. 20 - Prob. 20.142EPCh. 20 - Prob. 20.143EPCh. 20 - Describe the process by which blood...Ch. 20 - Prob. 20.145EPCh. 20 - Prob. 20.146EPCh. 20 - Prob. 20.147EPCh. 20 - Prob. 20.148EPCh. 20 - Prob. 20.149EPCh. 20 - Prob. 20.150EPCh. 20 - Prob. 20.151EPCh. 20 - Prob. 20.152EP
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- Which of the following events would have the strongest influence on the overall three-dimensional structure of a protein? Select one: a. Valines angle away from surrounding water molecules as the protein folds b. Two polypeptide strands, running in opposite directions, form hydrogen bonds with each other Oc. Another protein sticks to its outside d. The amine and carboxylic ends of the protein chain are left unreacted Oe. Three glycines are chained together Clear my choice Previous page esc ! 1 ← 2 3 W 3 E 38 $ 4 R 5 T 80 MacBook Pro A 6 Y & 7 U 8 I 9 4 1 O 0 P TO + ( W Next paarrow_forwardThe tertiary structure of a protein is established by: a. The sequence of amino acids in the protein b. The molecular weight of the protein c. The total number of amino acids in the protein d. The number of disulfide bridges in the protein e. The net charge of the the protein at physioloical pH.arrow_forwardWhich of the following statements is/are TRUE for globular proteins? A. sensitive to changes in pH & heat B. regular amino acid sequence C. soluble in water D. structural rolearrow_forward
- Which of the following is NOT TRUE about secondary structure in proteins? (More than one may apply) A. Stabilized by non-covalent bonds B. Is illustrated by DnaA molecules interacting in the ori C. Unravels at high temperatures when intramolecular non-covalent bonds are destroyed D. Occurs in a subregion of a protein E. Exemplified by beta sheets F. Describes the order of amino acids in a polypeptidearrow_forwardAt what level of protein structure does each of the following denaturation act? a. heat b. strong acid c. saturated salt solution d. organic solvents (e.g., alcohol or chloroform)arrow_forwardWhich of the following statement about quaternary structure of protein is correct? Select one: a. Quaternary structure is a force between different polypeptides. b. Hydrogen bond is an only force found in quaternary structure. c. Quaternary structure contains one polypeptide. d. Quaternary structure is an unfolded form of protein.arrow_forward
- Which of the following statements is incorrect? A.- the structure and charge of the proteins have direct effects on the rate of its migration through the gel matrix include b.- SDS is a type of a buffer with strong protein-denaturing effect and binds to the protein backbone at a constant molar ratio c.- SDS and polyacrylamide gel largely eliminates the influence of the structure and charge, and proteins are separated solely based on polypeptide chain length. d.When proteins are separated by electrophoresis through a gel matrix, smaller proteins appears at the lower portion of the gelarrow_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_forwardA. A macromolecule composed of one or more polypeptides B. The monomer of polypeptides. C. The specific sequence of amino acids in a polypeptide. D. Structure of coils and/or folds of a polypeptide strueture. E. Structure of polypeptide resulting from interactions between R-groups. Contributes to unique 3D shape of molecule. F. Two or more polypeptides interacting to form a single functional unit. 1. Protein 2. amino acid 3. primary structure 4. secondary structure 5. tertiary structure 6. quaternary structurearrow_forward
- Oftentimes, the major challenge in the determination of protein structure via X-ray crystallography is the production of good crystals. One common approach is to crystallize fragments of the whole protein instead of crystallizing the whole protein. If you were to cleave a protein into fragments that will still retain the folding of that fragment in the whole protein, where is the best location to perform the cleavage? O At the ends of each alpha helix. O At the ends of a protein motif. O At the points connecting protein domains. O At the ends of beta strands.arrow_forwardDescribe the levels of structure of a protein and tell how they would be affected by: a. Hydrolysis with 6M HCl (breaks peptide bond)b. Heating with mercaptoethanol (breaks hydrogen bonds)arrow_forwardIn a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains. Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY