BIOLOGY CUSTOM VERSION (NEW EDITION)
4th Edition
ISBN: 9781307156386
Author: BROOKER
Publisher: MCG/CREATE
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 3.6, Problem 2CC
Summary Introduction
To determine: The difference in the interaction between two proteins if the structure of one protein is altered.
Introduction: Tertiary or quaternary proteins are of different type like: globular proteins, enzymes and so on. These proteins interact or bind with each other by the different type of forces like (hydrogen bonds, Van der Waals forces, ionic bonds, and hydrophobic bonds). The interaction between an enzyme and its substrate or interaction between two globular proteins all these interactions include bond formation.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Cystic fibrosis (CF) is an inherited disorder caused by different types of mutations, many of which prevent ions from moving across cell membranes. Normally there are channel proteins that allow passage of the ions, but in patients with one kind of CF these proteins seem odd. Closer examination shows that these proteins display the correct amino acid sequence. However, they fail to do their job. A) Given that the primary structure of the protein is correct, what can you infer about the DNA sequence for the gene coding this protein on this patient, is there a mutation? Explain. B) Why is the primary structure insufficient to guarantee the proper function of the protein?
Why does a folded mutant protein aggregate rather than remain a misfolded monomer?
Assume that the translational error frequency, d, is 1 * 10–4. (a) Calculate the probability of making a perfect protein of 100 residues. (b) Repeat for a 1000-residue protein.
Chapter 3 Solutions
BIOLOGY CUSTOM VERSION (NEW EDITION)
Ch. 3.4 - Prob. 1CCCh. 3.4 - What type of reaction is the reverse of the one...Ch. 3.4 - Prob. 1BCCh. 3.5 - Prob. 1CCCh. 3.5 - Prob. 2CCCh. 3.6 - How many water molecules would be produced during...Ch. 3.6 - Prob. 2CCCh. 3.6 - Prob. 1EQCh. 3.6 - Prob. 2EQCh. 3.6 - CoreSKILL Explain the result that was crucial to...
Ch. 3.7 - Prob. 1CCCh. 3 - Molecules that are found in living cells and...Ch. 3 - The versatility of carbon that allows it to serve...Ch. 3 - Prob. 3TYCh. 3 - Prob. 4TYCh. 3 - Prob. 5TYCh. 3 - In contrast to other fatty acids, essential fatty...Ch. 3 - Prob. 7TYCh. 3 - The monomers of proteins are ___________, and...Ch. 3 - Prob. 9TYCh. 3 - Prob. 10TYCh. 3 - Explain the similarities and differences between...Ch. 3 - Prob. 2CQCh. 3 - Prob. 3CQCh. 3 - Discuss the differences between the various types...Ch. 3 - Prob. 2COQ
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
- (a) How many activation cycles are needed for a protein with 150 amino acids? (b) How many initiation cycles are needed for a protein with 150 amino acids? (c) How many elongation cycles are needed for a protein with 150 amino acids? (d) How many termination cycles are needed for a protein with 150 amino acids?arrow_forwardConsider a short peptide that forms an alpha-helix within a larger protein structure. Suppose that one glutamate residue at some specific position in the helix were mutated to a leucine residue. The mutation could either make the helix more stable, or less stable. i) Describe two situations in which a Glu-to-Leu mutation could make the helix more stable. ii) Describe two situations in which the Glu-to-Leu mutation could make the helix less stable. Explain briefly the basis for the stabilizing and destabilizing effect in all cases.arrow_forwardWhat is single-cell protein? Explain the reasons for the removal or reduction of nucleic acid in Single Cell Protein.arrow_forward
- A normal polypeptide and a mutant of the polypeptide were hydrolyzed by an endopeptidase under the same conditions. The normal and mutantpolypeptide differ by one amino acid. The fingerprints of the peptides obtained from the two polypeptides are shown below. What kind of amino acid substitution occurred as a result of the mutation? (That is, is the substituted amino acid more or less polar than the original amino acid? Is its pI lower or higher?) (Hint: Photocopy the fingerprints, cut them out, and overlay them.)arrow_forwardIn most cases, mutations in the core of a protein that replace a smaller nonpolar side chain in the wild-type (e.g., Ala, Val) with a larger nonpolar side chain (e.g., Leu, Ile, Phe, Trp) in the mutant, result in significant destabilization and misfolding of the mutant. What feature of the protein core explains this observation? Why would such a mutation prevent a protein from folding properly?arrow_forwardAssume that the translational error frequency, 8, is 1 × 10-4. (a) Calculate the probability of making a perfect protein of 100 residues. (b) Repeat for a 1000-residue protein.arrow_forward
- What makes the initiator tRNAmet so special? Does this have any impact on the amino acid sequence of all proteins?arrow_forwardThe sequence of kassinin, a tachykinin dodecapeptide from the African frog Kassina senegalensis, was determined. A single round of Edman degradation identifies Asp as the N-terminus. A second sample of the peptide is treated with chymotrypsin. Two fragments are released with the following amino acid compositions: fragment I (Gly, Leu, Met, Val) and fragment II (Asp2,Gln, Lys, Phe, Pro, Ser, Val). Next, a third sample of the peptide is treated with trypsin, which results in two fragments with the following amino acid compositions: fragment III (Asp, Pro, Lys, Ser) and fragment IV (Asp, Gln, Gly, Leu, Met, Phe, Val2). Treatment of another sample with elastase yields a single Gly residue and three fragments—fragment V (Leu, Met), fragment VI (Asp,Lys, Pro, Ser, Val), and fragment VII, which was sequenced: Asp–Gln–Phe–Val. A fourth sample was treated with CNBr, but the dodecapeptide was not cleaved.arrow_forwardShown below is an R loop prepared for electron microscopy by annealing a purified eukaryotic messenger RNA with DNA from a genomic clone containing the full-length gene corresponding to the mRNA. (a) How many exons does the gene contain? How many introns? (b) Where in this structure would you expect to find a 5′,5′-internucleotide bond? Where would you expect to find a polyadenylic acid sequence?arrow_forward
- Disulfide bonds have been shown to stabilize proteins (i.e., make them less likely to unfold). Consider the cases shown schematically below for two variants of the same protein. In case #1 the disulfide forms between Cys residues that have been introduced near the protein N- and C-termini, and in case #2 the disulfide forms between Cys residues that have been introduced in the middle of the protein sequence. Which protein is likely to be more stable? (Note: Assume the disulfide bond is intact in both the unfolded and folded states). Explain your reasoning.arrow_forwardBased on the N-terminal amino acid sequence, what is the approximate half-life of the protein after methionine is cleaved off?arrow_forwardA recent genome sequencing project for the bacterium Burkholderia mallei has identified a new protein with high similarity to the lysylphosphatidylglycerol flippase enzyme. A short section of the new protein sequence is shown below. TVEVNAPGDVQKALSELQQINDGRLDIRI (a) Are any reverse turns likely to be present? Explain your answer. (b) Are any beta-strands likely to be present? Explain your answer. (c) Are any alpha helices likely to be present? Explain your answer. (d) Is any supersecondary structure likely to be present? Explain your answer. (e) Identify two residues that are likely to be buried in the core of the folded protein. Explain your answer. (f) Identify two residues that are likely to be hydrogen bonded to each other. Explain your answer.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Human Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage Learning
Human Heredity: Principles and Issues (MindTap Co...
Biology
ISBN:9781305251052
Author:Michael Cummings
Publisher:Cengage Learning
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY