Biology (MindTap Course List)
11th Edition
ISBN: 9781337392938
Author: Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. Berg
Publisher: Cengage Learning
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Chapter 3, Problem 17TYU
EVOLUTION LINK Each amino acid could potentially exist as one of two possible enantiomers, known as the D-form and the L-form (based on the arrangement of the groups attached to the asymmetric α carbon). However, in all organisms, only L-amino acids are found in proteins. What does this suggest about the evolution of proteins?
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Consider the 20 standard amino acids and their structures. Choose a set of 6 amino acids that you think could theoretically be eliminated from existence and still allow proteins to fold, function, and support life with the remaining 14. Eliminating amino acids from existence would result in a need for changes to the amino acid sequence of proteins, however your choices of amino acids to eliminate should result in minimal changes to the way proteins are currently structured and function. For each amino acid that you propose to eliminate defend your choice with a 2-3 point explanation using reasoning. Your answer should be no longer than 1.5 pages in length and you should start a new paragraph for each amino acid that you select to be eliminated.
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What kind of bond would you expect between the side chains of the following amino acids?(a) Cysteine and cysteine(b) Alanine and leucine(c) Aspartic acid and asparagine(d) Serine and lysine
Chapter 3 Solutions
Biology (MindTap Course List)
Ch. 3.1 - Describe the properties of carbon that make it the...Ch. 3.1 - Define the term isomer and distinguish among the...Ch. 3.1 - Identify the major functional groups present in...Ch. 3.1 - Explain the relationship between polymers and...Ch. 3.1 - What are some of the ways that the features of...Ch. 3.1 - Prob. 2CCh. 3.1 - Prob. 3CCh. 3.1 - Prob. 4CCh. 3.1 - Prob. 5CCh. 3.2 - Distinguish among monosaccharides, disaccharides,...
Ch. 3.2 - VISUALIZE Draw simple sketches comparing the...Ch. 3.3 - Distinguish among fats, phospholipids, and...Ch. 3.3 - Prob. 1CCh. 3.3 - Explain why the structure of phospholipids enables...Ch. 3.4 - Give an overall description of the structure and...Ch. 3.4 - Prob. 8LOCh. 3.4 - Distinguish among the four levels of organization...Ch. 3.4 - Prob. 1CCh. 3.4 - Prob. 2CCh. 3.5 - Describe the components of a nucleotide. Name some...Ch. 3.5 - VISUALIZE Sketch a pyrimidine nucleotide subunit...Ch. 3.6 - Compare the functions and chemical compositions of...Ch. 3.6 - How can you distinguish a pentose sugar from a...Ch. 3 - Prob. 1TYUCh. 3 - VISUALIZE The structures depicted are (a)...Ch. 3 - Prob. 3TYUCh. 3 - The synthetic process by which monomers are...Ch. 3 - A monosaccharide designated as an aldehyde sugar...Ch. 3 - Structural polysaccharides typically (a) have...Ch. 3 - Saturated fatty acids are so named because they...Ch. 3 - Fatty acids in phospholipids and triacylglycerols...Ch. 3 - Which of the following levels of protein structure...Ch. 3 - Which of the following associations between R...Ch. 3 - Each phosphodiester linkage in DNA or RNA includes...Ch. 3 - PREDICT Do any of the amino acid side groups shown...Ch. 3 - PREDICT Like oxygen, sulfur forms two covalent...Ch. 3 - Hydrogen bonds and van der Waals interactions are...Ch. 3 - EVOLUTION LINK In what ways are all species alike...Ch. 3 - EVOLUTION LINK The total number of possible amino...Ch. 3 - EVOLUTION LINK Each amino acid could potentially...
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- Refer to the figure below. Replacing lysine with another amino acid in the protein may alter the shape and function of the protein. Replacing lysine with which type(s) of amino acid(s) would lead to the least amount of change in the tertiary structure of this protein? Explain.arrow_forwardupvote guaranteedarrow_forwardA mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)arrow_forward
- Hundreds of thousands of proteins have been discovered inliving organisms. Yet, as astonishing as this diversity is,these molecules constitute only a small fraction of thosethat are possible. Calculate the total number of possibledecapeptides (molecules with 10 amino acid residues linkedby peptide bonds) that could be synthesized from the 20standard amino acids. If you were to spend 5 minutes writing out the molecular structure of each possible decapeptide,how long would the task take?arrow_forward(a) A protein is found to be a tetramer of identical subunits. Name two symmetries possible for such a molecule. What kinds of interactions (iso logous or heterologous) would stabilize each? (b) Suppose a tetramer, like hemoglobin, consists of two each of two types of subunits, a and B. What is the highest symmetry now possible?arrow_forwardWhich of the following statments are correct about protein evolution (select all that apply)? A. Most proteins only contain one structural domain B. Most naturally occurring mutations in a protein domain will substantially disrupt the structure C. Many individual doamins contain specialized functions that may be swapped between proteins D. It is the cummulative effects of mutations in a domain that lead to new structures and functions. E. Only mixing and matching of domains allow proteins to create new structuresarrow_forward
- Lysine is one of the 20 amino acids that found in protein. Draw the form (s) of lysine that would exist at pH 5.0. pK (α-carbonyl group) = 2.2 ; pK (α-amino group) = 9.2 ; pK (R group) = 10.8arrow_forwardLook at Table 18.3 and identify the type of noncovalent interaction expected between the side chains of the following pairs of amino acids:(a) Glutamine and serine (b) Isoleucine and proline(c) Aspartate and lysine (d) Alanine and phenylalaninearrow_forwardUnconfirmed rumour has it that the NASA Curiosity rover may have found evidence for the existence of life on the Mars surface in the form of traces of molecules that seem to resemble an amino acid. While the scientific soundness of these claims remains fiercely debated amongst researchers the initial analysis of the alien amino acid suggested that it carried three different ionisable groups. This included an alpha carboxyl group with a pka of 2.30 but surprisingly no alpha amino group. In addition the amino acid contained both the side chains found in glutamate and the one found in lysine. i) In less than 50 words provide a general explanation on how you can determine the pI of the alien amino acid. ii) Use the pka table below to determine the isoelectric point of the alien amino acid to two decimal places, show your working out and state the final result in a full sentence.arrow_forward
- Unconfirmed rumour has it that the NASA Curiosity rover may have found evidence for the existence of life on the Mars surface in the form of traces of molecules that seem to resemble an amino acid. While the scientific soundness of these claims remains fiercely debated amongst researchers the initial analysis of the alien amino acid suggested that it carried three different ionisable groups. This included an alpha carboxyl group with a pka of 2.30 but surprisingly no alpha amino group. In addition the amino acid contained both the side chains found in glutamate pka 4.25 and the one found in lysine pka 10.79. i) In less than 50 words provide a general explanation on how you can determine the pI of the alien amino acid. ii) Use the pka values to determine the isoelectric point of the alien amino acid to two decimal places, show your working out and state the final result in a full sentence.arrow_forwardDraw the two amino acids serine and alanine, and a dipeptide that could be formed by combining these two amino acids (ala-ser). Draw these molecules at a pH=7. In peptide nomenclature the amino terminus is on the left and the carboxyl terminus is on the right. 1. How many waters were released by formation of this dipeptide from individual amino acids? [ Select ] 2. How many hydrogen bond donors does your dipeptide have? [ Select ] 3. If you were to draw this dipeptide at a pH :1, would the number of hydrogen bond donors change? [ Select ]arrow_forwardSuppose that there is a protein consisting of two polypeptide chains with the given sequences in the picture. What will be the expected result if a biochemist does an end-group analysis to identify the N and C terminal residues of the protein? Explain why.arrow_forward
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