Modified Mastering Biology With Pearson Etext -- Standalone Access Card -- For Biological Science (7th Edition)
7th Edition
ISBN: 9780135276556
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Greg Podgorski, Emily Taylor, Jeff Carmichael
Publisher: PEARSON
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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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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-M
It would be useful to have a string-matching method that can be used to compare proteins and identify those that are similar to each other. Can you explain its role? In what ways might your claim be supported?
Describe how to predict intrinsically disordered proteins (IDP) and intrinsically disordered regions (IDR) from amino acid sequences.
Chapter 3 Solutions
Modified Mastering Biology With Pearson Etext -- Standalone Access Card -- For Biological Science (7th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - What type of information is used to direct...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 9TYPSSCh. 3 - Prob. 12PIATCh. 3 - Prob. 13PIATCh. 3 - Recall that proline often introduces kinks in the...Ch. 3 - SOCIETY Based on the experiment in question 15,...
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- 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. Determine the intracellular binding partners of the protein of interest.arrow_forwardDescribe how proteins are sequenced, and explain why sequence determination is importantarrow_forwardDescribe how two protein sequences are aligned, and how one can determine whether that alignment is significant.arrow_forward
- Consider the proteins in Figure 1. Assume they are treated with chymotrypsin to cut them into fragments, and then the fragments are separated by gel electrophoresis. What would the fragment patterns look like in the gel for the three different proteins, assuming we can separate polypeptides that differ in size by very small amounts? Complete Figure 2 below to show the location of the uncut polypeptides (- enzyme lanes) and the cut fragments (+ enzyme lanes).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_forwardDescribe the strategies that could be used to design a protein that could exist.arrow_forward
- Suppose that you are tasked to determine the protein concentration of an unknown protein solution via Bradford assay. You prepared six solutions of bovine serum albumin (BSA) with different concentrations. The initial concentration of the BSA stock solution is 7.50 mg/mL. Approximately 200 µL of Bradford Reagent was added to each of these solutions and the absorbance at 595 nm was taken after 5 minutes. See the table below for data on the standard solutions. Standard # A595 BSA conc (mg/mL) 0.000 0.158 2 1.125 0.291 2.250 0.372 4 3.375 0.503 5 4.500 6 5.625 0.675 Determine the protein concentration, in mg/mL, of the unknown solution if its absorbance at 595 nm was 0.248. Note: Final answer format must be x.xx (two decimal places). Round off only in the final answer. Do not round off in the middle of calculation.arrow_forwardGive typed explainarrow_forwardIf a bacterial protein is 3,300 amino acids long, how many nucleotidepairs long is the gene sequence that codes for it?arrow_forward
- Assume you isolated muscle proteins from three different organisms: one from a fish in the Atlantic Ocean, one from a fish in the Pacific Ocean, and one from an Eastern European deer species. Based on the evolutionary relationships of the three organisms mentioned above, which two samples would you expect to have a similar protein pattern when you perform Polyacrylamide gel electrophoresis? Explain your response briefly.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_forwardIf you know the sequence of amino acids in a protein, what does the genetic code table allow you to infer about the sequence of base pairs in the gene that specifies that protein?arrow_forward
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