Biological Science (6th Edition)
6th Edition
ISBN: 9780321976499
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Emily Taylor, Greg Podgorski, Jeff Carmichael
Publisher: PEARSON
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Question
Chapter 3, Problem 5TYU
Summary Introduction
To analyze:
Considering a cell put to use 10 or 20 amino acids into peptides that are five residues long, determine the effect on protein diversity.
Introduction:
Proteins are
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Describe the common strategy (steps) for protein sequencing, starting with a biological sample containing many cell and biochemical substances.
How prevalent are disulfide links in proteins? Why do the disulfide links need to be broken prior to sequencing? How can they be chemically broken?
A very common molecular biology research method is to analyze cell or tissue homogenates by SDS-polyacrylamide gel electrophoresis and immunoblotting (Western blot). What can we learn about a protein of interest from this type of analysis?
More than one answer is correct.
Options:
Determine the tertiary structure of the protein of interest.
Determine or verify the molecular weight of the protein of interest.
Compare the levels of the protein of interest in two different cell types.
Determine the amino acid sequence from the product ion spectrum.
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Chapter 3 Solutions
Biological Science (6th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - 2. What type of bond is directly involved in the...Ch. 3 - What type of information is used to direct...Ch. 3 - 4. What is an active site?
a. the location in an...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 8TYUCh. 3 - Prob. 9TYPSSCh. 3 - 10. Make a concept map (see BioSkills 12) that...
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- Suppose that there is an unknown protein that underwent Edman sequencing method. From N- terminal determination, a biochemist found out that there are two N-terminal amino acid residues, V and G. What is the original sequence of the protein given the following peptide fragments: after digestion with Chymotrypsin: G-L-S-R-G-M-w V-A-L-F Q-L-Y L-R-V-W G-M-V-E-A-D-I-P K-S-P-E-M-T-W R-M-A-S-E-K-P-G-H after digestion with Trypsin: P-G-H V-W-G-M-V-E-A-D-I-P M-A-S-E-K G-M-W-Q-L-Y-L-R S-P-E-M-T-W-R G-L-S-R V-A-L-F-K after digestion with Cyanogen Bromide: T-W-R-M W-Q-L-Y-L-R-V-W-G-M V-E-A-D-I-P A-S-E-K-P-G-H V-A-L-F-K-S-P-E-M G-L-S-R-G-Marrow_forwardOutline 5 factors to be considered when performing a similarity search with a short peptide/nucleotide sequence.arrow_forwardDescribe how proteins are sequenced, and explain why sequence determination is importantarrow_forward
- Explain why similarities between protein sequences (orbetween DNA sequences) can be used as a measure of relativerelatedness.arrow_forwardIf an average amino acid is 110Da, how many amino acids would you predict to have in a polypeptide that is 65,000 Daltons in size? How many nucleotides would this be if you were looking for the gene size?arrow_forwardDescribe how two protein sequences are aligned, and how one can determine whether that alignment is significant.arrow_forward
- Attatched is shown a boxshaded sequence alignment of Horse (top line) and myoglobin (second line). Explain the significance of the black, grey and white colours in your boxshade file. Use the first ten amino acids pairs in the line-up to illustrate your answer.arrow_forwardGene editing is also used to explore the structure and function ofproteins. For example, changes can be made to the coding sequenceof a gene to determine how alterations in the amino acid sequenceaffect the function of a protein. Let’s suppose that you areinterested in the functional importance of a particular glutamicacid (an amino acid) within a protein you are studying. By geneediting, you make mutant proteins in which the glutamic acidcodon has been changed to other codons. You then test the encodedmutant proteins for functionality. The results are as follows: FunctionalityNormal protein 100%Mutant proteins containingTyrosine 5%Phenylalanine 3%Aspartic acid 94%Glycine 4%From these results, what would you conclude about the…arrow_forwardYou are a molecular biologist studying a defective human protein that is known to be a cause of a rare cancer. You isolate the suspected protein from a person with this cancer and compare it to the same protein in a person without the cancer. You discover that the protein isolated from the cancer patient is slightly smaller in size when compared to the protein from the unaffected patient. Furthermore, you discover that the protein from the cancer patient differs in almost every amino acid starting after the 23rd amino acid. What is the likely explanation?arrow_forward
- Explain how a multiple sequence alignment can identify functional sites in a genetic sequence.arrow_forwardSDS-PAGE and Agarose gel electrophoresis can both be used to separate proteins or protein- complexes based on their size. Separation of a multi-subunit protein complex by SDS-PAGE resulted in two bands with molecular weights of 86 KDa and 136 KDa, while separation of the same complex using Agarose gel electrophoresis resulted in two bands with molecular weights of 222 KDa and 444 KDa. Based on this information, which of the following statements is most likely to be correct? O The complex has a molecular weight of 222 KDa O The complex exists as a dimer of homo-dimers O The complex exists as a dimer of hetero-dimers SE O The complex exists as a trimer, but the individual protein subunits are covalently crosslinked to each otherarrow_forwardYou are a molecular biologist studying a defective human protein that is known to be the cause of a rare cancer. You isolate the suspected protein from a person with this cancer and compare it to the same protein in a person without the cancer. You discover that the protein isolated from the cancer patient is slightly smaller in size when compared to the protein from the unaffected patient. Furthermore, you discover that the protein from the cancer patient differs in almost every amino acid starting after the twenty-third amino acid. What is the likely explanation?arrow_forward
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