Biology 2e
2nd Edition
ISBN: 9781947172517
Author: Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher: OpenStax
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Textbook Question
Chapter 3, Problem 23CTQ
Amino acids have the generic structure seen below, where R represents different carbon-based 
side chains.
Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
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Amino acids have the generic structure, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
Suppose that the given peptide below is a segment in a globular protein's primary structure. Determine what would most likely be the type of secondary structure that it will form. Explain.
T-L-S-A-R-I-D-V
Amino acids have the generic structure, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins. Make an imaginary peptide chain or protein molecule.
Chapter 3 Solutions
Biology 2e
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- Below is the structure of glycine. Draw a tripeptide composed exclusively of glycine. Label the N-terminus and C-terminus. Draw a box around the peptide bonds.arrow_forwardDraw the generalized structure of an amino acid, and a peptidebond that connects them in proteinsarrow_forwardExplain why amino acid can increase blood glucose. Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number. Alanyl-phenylalanine- aspartate- cysteine Threonyl- Isoleucyl-methionyl- leucine Lysyl-alanine -Phenylalanyl-tyrosyl- serinearrow_forward
- 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_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_forwardName and draw the structure of two charged amino acidsarrow_forward
- Give the names of the 20 Common Amino Acids and draw the structure of each.arrow_forwardDescribe the amino acid illustrated above (at pH = 7.0). (the following amino acid at pH = 7 (aqueous form): (COO-)–CH(NH3+)–CH2–(COO-)) it is a non-polar, positively-charged amino acid it is a polar, positively-charged amino acid it is a polar, uncharged amino acid it is a polar, negatively-charged amino acid it is a non-polar, negatively-charged amino acidarrow_forwardIn this sequence: Histidine - Alanine - Aspartic acid - Leucine tetrapeptide (show using your model how the water is released). Show the peptide bonds on your figure. See figure 1arrow_forward
- Suppose that the sequence is part of a larger globular protein. Consider the probable location, either on the external surface or the interior of the protein, of each of the amino acid residues. The table gives the hydropathy index values for selected amino acids in the peptide. Amino acid Hydropathy index alanine 1.8 isoleucine 4.5 threonine -0.7 glutamine -3.5 lysine -3.9 aspartate -3.5arrow_forwardGive an example of a protein that has quaternary structure. How many polypeptide chains are present in this protein?arrow_forwardRefer 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 your answer.arrow_forward
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