Campbell Essential Biology (7th Edition)
7th Edition
ISBN: 9780134765037
Author: Eric J. Simon, Jean L. Dickey, Jane B. Reece
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 3, Problem 19PS
Imagine that you have produced several versions of lactase, each of which differs from normal lactase by a single amino acid. How could you determine which versions alter the protein’s shape?
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Draw the structure of lactose and name its constituent monosaccharides. What enzyme is responsible for the degradation of lactose into its component parts?
Your friend has discovered a protein that they suspect is glycosylated. They decide to perform a series of tests to determine the nature of the oligosaccharide.
Assuming/Knowing the following:
Fucose molecular weight is approximately 164
Galactose molecular weight is approximately 180
GalNAc molecular weight is approximately 221
Mannose molecular weight is approximately 180
Sialic Acid molecular weight is approximately 309
Neuraminidase cleaves before a Sialic Acid (Sialic Acid and anything after leaves the protein)
Beta-galactosidase cleaves after a Galactose (Galactose and anything before remains on the protein)
Peanut Agglutinin binds to GalNAc
Concanavalin A binds to Mannose
Hemagglutinin binds to Sialic Acid
Based on preliminary results, they suspect that the oligosaccharide is 7 glycosides long and weighs a total of 1414 g/mol
They carried out the following experiments: they treated the protein with either a glycosidase or a lectin, and then pelleted the protein using…
Lactose permease, a protein of E. coli, is composed of a singlepolypeptide that is 417 amino acids in length. By convention, theamino acids within a polypeptide are numbered from the aminoterminalend to the carboxyl-terminal end. Are the following questionsabout lactose permease true or false?A. Because the sixty-fourth amino acid is glycine and the sixty- eighth amino acid is aspartic acid, the codon for glycine,64, is closer to the 3′ end of the mRNA than the codon for aspartic acid, 68.B. The mRNA that encodes lactose permease must be greater than1241 nucleotides in length.
Chapter 3 Solutions
Campbell Essential Biology (7th Edition)
Ch. 3 - One isomer of methamphetamine is the addictive...Ch. 3 - Monomers are joined together to form larger...Ch. 3 - Polymers are broken down into monomers through the...Ch. 3 - Prob. 4SQCh. 3 - When two molecules of glucose (C6H12O6) are joined...Ch. 3 - One molecule of dietary fat is made by joining...Ch. 3 - Prob. 7SQCh. 3 - Prob. 8SQCh. 3 - Prob. 9SQCh. 3 - Most proteins can easily dissolve in water. Where...
Ch. 3 - Prob. 11SQCh. 3 - A glucose molecule is to _____ as a nucleotide is...Ch. 3 - Name three similarities between DNA and RNA. Name...Ch. 3 - Prob. 14SQCh. 3 - For each statement, identify which major theme is...Ch. 3 - For each statement, identify which major theme is...Ch. 3 - Prob. 17IMTCh. 3 - Scientists at the U.S. Food and Drug...Ch. 3 - Imagine that you have produced several versions of...Ch. 3 - Prob. 20PSCh. 3 - Prob. 21BSCh. 3 - Heart disease is the leading cause of death among...Ch. 3 - Each year, industrial chemists develop and test...
Additional Science Textbook Solutions
Find more solutions based on key concepts
11. In the early 1800s, French naturalist Jean Baptiste Lamarck suggested that the best explanation for the rel...
Campbell Biology: Concepts & Connections (8th Edition)
Police Captain Jeffers has suffered a myocardial infarction. a. Explain to his (nonmedically oriented) family w...
Human Physiology: An Integrated Approach (8th Edition)
6. How can you use the features found in each chapter?
Human Anatomy & Physiology (2nd Edition)
On what molecule does the anticodon appear? Explain the role of this molecule in protein synthesis.
Human Physiology: An Integrated Approach (7th Edition)
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Identify the parts of the heterotrimeric G-protein shown in the image. Barrow_forwardAmino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?arrow_forwardBriefly describe the structural differences for each pair listed: A) Glycogen and Cellulose B) Lactose and Sucrosearrow_forward
- There are 20 standard amino acids and only 10 major monosaccharides in eukaryotes, yet there are so many more possible combinations of monosaccharides in a hexasaccharide than amino acids in a hexapeptide. Explain this observation.arrow_forwardb-Galactosidase is an enzyme that hydrolyses only b(1,4)linkages of lactose. An unknown trisaccharide is convertedby b-galactosidase into maltose and galactose. Draw thestructure of the trisaccharidearrow_forwardHow many carbon atoms are present in the R group in each of the following standard amino acids? Please see picture. Thank you!arrow_forward
- Proteins are essential to most processes in the human body. Given your understanding of the M phase of the life cycle, please discuss two different protein dependent processes associated with this phase. Make sure you provide specific details about the chosen processes.arrow_forwardWhy is lactose a reducing sugar while sucrose is a non-reducing sugar? Explain clearly. Please support the answer with an illustration.arrow_forwardThe carbohydrate portion of some glycoproteins may serve as a cellular recognition site. To perform this function, the oligosaccharide moiety must have the potential to exist in a large variety of forms. Which can produce a greater variety of structures: oligopeptides composed of five different aminoacid residues, or oligosaccharides composed of five different monosaccharide residues? Explain.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_forwardImagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. In the table below are four possibilities for what R, and R, might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ threonine cysteine glutamine arginine cysteine tyrosine phenylalanine glutamate specific interaction? Oyes no yes O no O yes O no Oyes O no name of specific interaction 0 0 0 0 Xarrow_forwardhow does the protein environment surrounding an amino acid chain affect its chemical properties?Consider the carboxyl group on an asparate side chain in the following environments in a protein. Rank in order these environments from the highest to the lowest proportion of carboxyl groups in the -COO- form.that is in terms of pKas. 1. an aspartate side chain on the surface of protein with no other ionizable groups nearby. 2. an aspartate side chain buried in a hydrophobic pocket on the surface of a protein 3. an asparate chain in a hydrophobic pocket adjacent to a glutamte side chain 4. an asparate side chain in a hydrophobic porket adjacent to a lysine side chain.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
Macromolecules | Classes and Functions; Author: 2 Minute Classroom;https://www.youtube.com/watch?v=V5hhrDFo8Vk;License: Standard youtube license