EBK BIOLOGY
4th Edition
ISBN: 8220102797376
Author: BROOKER
Publisher: YUZU
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 14.1, 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.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Suggest probable consequences of the following real or possible hemoglobinmutations. [Note: as shown](a) At β146 (HC3) His → Asp(b) At β92 (F8) His → LeuIn each case, indicate whether a single-nucleotide change is sufficient forthe 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
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.
Chapter 14 Solutions
EBK BIOLOGY
Ch. 14.1 - Consequences of Mutations Concept Check: Based on...Ch. 14.1 - Prob. 2CCCh. 14.1 - Prob. 3CCCh. 14.2 - Prob. 1EQCh. 14.2 - Prob. 2EQCh. 14.2 - Prob. 3EQCh. 14.2 - Prob. 1CCCh. 14.2 - Prob. 2CCCh. 14.3 - DNA Repair Concept Check: Which components of the...Ch. 14.3 - Why is this person so sensitive to sunlight?...
Ch. 14.4 - Prob. 1CCCh. 14.4 - Prob. 1BCCh. 14.4 - Prob. 2CCCh. 14.4 - Prob. 3CCCh. 14.4 - Prob. 4CCCh. 14 - Prob. 1TYCh. 14 - Prob. 2TYCh. 14 - Prob. 3TYCh. 14 - Prob. 4TYCh. 14 - Prob. 5TYCh. 14 - The Ames test a. provides a way to determine if...Ch. 14 - Xeroderma pigmentosum a. is a genetic disorder...Ch. 14 - Prob. 8TYCh. 14 - Prob. 9TYCh. 14 - Prob. 10TYCh. 14 - Prob. 1CQCh. 14 - Prob. 2CQCh. 14 - Prob. 3CQCh. 14 - Prob. 1COQCh. 14 - Distinguish between spontaneous and induced...
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
- 1CFD CALCIUM-FREE CALMODULIN How long is the protein’s primary sequence?Does this protein have any secondary, tertiary and/or quaternary structures present?Are there any molecular additions to this protein that are not amino acarrow_forwardIf a new isolated protein called STICKY and this STICKY protein contains a bHLH domain. Now, how we predict the function of STICKY and the rationale for the importance of these domains in the STICKY function?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_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_forwardGT 3 A. Write the structure of the pentapeptide GLDSC. B. What is the complete name of this pentapeptide? Show a tertiary structure of ACGGC after a disulfide bond forms. A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin; the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C- terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn-Thr-Trp-Met-lle-Lys Gly-Tyr-Met-Gln-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen bromide treatment Gln-Phe Val-Leu-Gly-Met lle-Lys-Gly-Tyr-Met Ser-Arg-Asn-Thr-Trp-Metarrow_forward.A protein gives a single band on SDS gel electrophoresis, as shown in lanes 1 and 2 below. There is little if any effect from addingarrow_forward
- Which statements are true? Explain why or why not.1 Each strand in a β sheet is a helix with two aminoacids per turn.2 Intrinsically disordered regions of proteins can beidentified using bioinformatic methods to search genes forencoded amino acid sequences that possess high hydro-phobicity and low net charge.3 Loops of polypeptide that protrude from the sur-face of a protein often form the binding sites for other mol-ecules.4 An enzyme reaches a maximum rate at high sub-strate concentration because it has a fixed number ofactive sites where substrate binds.5 Higher concentrations of enzyme give rise to ahigher turnover number.6 Enzymes that undergo cooperative allosteric tran-sitions invariably consist of symmetric assemblies of mul-tiple subunits.7 Continual addition and removal of phosphatesby protein kinases and protein phosphatases is wastefulof energy—since their combined action consumes ATP—but it is a necessary consequence of effective regulation byphosphorylation.arrow_forwardThe figure shows an example of a thermal denaturation plot. The melting temperature (Tm) is the midpoint of the temperature range over which denaturation occurs. Percent unfolded 100 80 60 40 20 0 20 Tm 40 60 Temperature (°C) 80 100arrow_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_forward
- The mutation in hemoglobin at B82 Lys → Asp results in lowered O,-binding affinity compared to normal hemoglobin. B82 is one of the residues that lines the 2,3-BPG binding site (see Figure 7.29; B82 is adjacent to His143). Based on the location of this residue and the differences between Lys and Asp, sug- gest a rationale for the observed reduction in Oz-binding affinity.arrow_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_forwardPart C Using the values of pKas in the table below, calculate the pI for DTLH. Properties of some amino acids found in proteins Name Aspartic acid Abbreviations: 1- and 3- letter codes D, Asp Histidine H, His Leucine L, Leu Threonine T, Thr ΓΙ ΑΣΦ Submit pKa of a-COOH pKa of a-NH3+ pKa of lonizing Group Group Side Chain Express your answer to two significant figures. Request Answer 2.1 1.8 2.4 2.6 ? 9.8 9.2 9.6 10.4 3.9 6.0arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Mitochondrial mutations; Author: Useful Genetics;https://www.youtube.com/watch?v=GvgXe-3RJeU;License: CC-BY