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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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_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_forwardAmino 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.arrow_forward
- Together, these monomers make up what type of polymer (macromolecule)? List at least three (broad) functions that these macromolecules can perform. What is an example protein that we’ve discussed that uses of these functions? Using R as the side chain, draw the basic structure of an amino acid.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.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_forwardFor the protein given in the attached picture: Write the name of these 5 amino acids corresponding to their abbreviation of 3 letters. Describe precisely how the functional groups in the amino acids are involved in bonding between two successive amino acids in the protein.arrow_forward
- Compare the molecular property of amino acids and their roles in protein folding. Hydrophilic acids Arginine Asparagine Aspartic Acid Cysteine Glutamic acid Glutamine Glycine Histidine Lysine Serine Threonine hydrophobic acids Alanine Isoleucine Leucine Methionine Phenylalanine Proline Tryptophan Tyrosine Valinearrow_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_forwardSuppose 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_forward
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