Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
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Chapter 15.1, Problem 1CC
Consequences of Mutations
Concept Check: Based on the fiber-like structures seen in part (c) of this figure, what aspect of hemoglobin structure does a glutamic acid at the sixth position in normal β-globin prevent? Speculate as to how the charge of this amino acid may play a role.
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Using the quarternary structure of hemoglobin shown inFigure 9-3(d), explain in structural terms how a mutation in the β subunit protein could be suppressed by amutation in the a subunit gene.
. Suggest probable conseauences of the following real or possible hemoglobin
mutations.
(a) At B146 (HC3) His → Asp
(b) At B92 (F8) His Leu
In each case, tell whether a single-nucleotide change is sufficient for the
mutation.
-. A schematic structure of the subunit of hemerythrin (an oxygen-
binding protein from invertebrate animals) is shown below.
(a) It has been found that in some of the a-helical regions of
hemerythrin, about every third or fourth amino acid residue is a
hydrophobic one. Suggest a structural reason for this finding.
(b) What would be the effect of a mutation that placed a proline
residue at point A in the structure?
A
Fe
Chapter 15 Solutions
Biology
Ch. 15.1 - Consequences of Mutations Concept Check: Based on...Ch. 15.1 - Prob. 2CCCh. 15.2 - Prob. 1EQCh. 15.2 - Prob. 2EQCh. 15.2 - Prob. 3EQCh. 15.2 - Prob. 1CCCh. 15.3 - DNA Repair Concept Check: Which components of the...Ch. 15.3 - Why is this person so sensitive to sunlight?...Ch. 15.4 - Prob. 1CCCh. 15.4 - Prob. 2CS
Ch. 15.4 - Prob. 2CCCh. 15.4 - Prob. 3CCCh. 15.4 - Prob. 4CCCh. 15 - Prob. 1TYCh. 15 - Prob. 2TYCh. 15 - Prob. 3TYCh. 15 - Prob. 4TYCh. 15 - Prob. 5TYCh. 15 - The Ames test a. provides a way to determine if...Ch. 15 - Xeroderma pigmentosum a. is a genetic disorder...Ch. 15 - Prob. 8TYCh. 15 - Prob. 9TYCh. 15 - Prob. 10TYCh. 15 - Prob. 1CQCh. 15 - Prob. 2CQCh. 15 - Prob. 3CQCh. 15 - Prob. 1COQCh. 15 - Distinguish between spontaneous and induced...
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- Myoglobin stores O2 in muscle tissue to be used by the mitochondria only when the cell is in oxygen debt, whereas hemoglobin can effectively transport O2 from the lungs and deliver it discriminately to cells in need of O2. Describe the structural features that allow these two proteins to accomplish separate functions.arrow_forwardThe proximal histidine residues have been replaced by glycine residues by mutation of the cloned genes for both the α and β subunits of hemoglobin. With the tetrameric mutant hemoglobin (all subunits being mutant, α H F8 G, β H F8 G), it was found that the “proximal” coordination bonds to hemes in the mutant protein could be replaced by having the small molecule imidazole in the buffers. Oxygen binding curves for the tetrameric mutant hemoglobin were measured. A. The degree of cooperativity in oxygen binding for the mutant hemoglobin (with imidazole present) would be expected to 1) increase 2) decrease 3) not be affected) compared with the normal protein. B. Justify your answer to part A in terms of what you know about the structural basis of cooperativity in hemoglobin. C. How would the Hill coefficient for the mutant be expected to change compared with nH for normal hemoglobin, which is ~3?arrow_forwardGiven: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?arrow_forward
- Genetics of man question:Describe the molecular genetics analysis for the GATA binding protein gene and consider the possibility of lethality and functional redundancy and experimental strategies to address possibilities.arrow_forwardАСTIVITY For each of the 4 regulatory states of the lac shown in the following diagram, answer the following questions: оperon 1) Is glucose present? 2) Is lactose present? Synthesis of lac MRNA? Glucose present? Lactose present? NO Repressor y a NO CAMP-CRP complex y YES Transcription i p o y NOarrow_forwardaestion How does myoglobin minimize oxidation of the Fe(II) when the heme binds to oxygen? Select one: a. the distal His E7 forms a hydrogen bond to the bound molecular oxygen O b. the oxygen binding site is buried in the hydrophobic core away from water O c. the proximal His F8 forms a coordinate bond to Fe(II), which inhibits oxidation O d. nonpolar interactions with residues Val E11 and Phe CD1 limit oxidation by oxygen Oe. the heme shifts to a planar structure that traps iron in a +2 oxidation state Clear my choicearrow_forward
- . The process of a protein folding from an inactive unfolded structure to the active folded structure can be represented by the following equation: unfolded protein = folded protein The values of AH and AS° for the folding of the protein lysozyme are: AH = -280 kJ/mol AS = -790 J/mol · K (a) Calculate the value of AG for the folding of lysozyme at 25 °C. (b) At what temperature would you expect the unfolding of lysozyme to become favorable?arrow_forwardPlease fill in the following blanks with the options that correctly finishes the sentence. a. At a low O₂ pressure the [Select] hemoglobin is in a [Select] [Select] [Select] 9 [Select] " bond with [Select] heme, and the protein's central channel is [Select] b. The proximal histidine forms a(n) [Select] state is stabilized. In this conformation state, the heme prosthetic groups is each subunit's heme is more likely to be the proximal histidine is [Select ] bond with while the distal histidine forms a(n) [Select] to thearrow_forwardOnce the chains of peptides that make up lysyl-tRNA synthetase protein are synthesized in ribosomes, lysyl-tRNA synthetase needs to have the proper active site in order to perform its function, explain the process of protein folding necessary to have a proper 3-D structure, include effect of thermodynamics and different states in folding, including what happen when there are prolines that form peptide bonds with other amino acids, and any disulfide bridgesarrow_forward
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