Chemical Basis of Bioengineering I

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Polypeptide Chain

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Chemical Basis of Bioengineering I

Definition

A polypeptide chain is a linear sequence of amino acids linked together by peptide bonds, forming the primary structure of proteins. These chains can vary in length and composition, leading to the immense diversity of proteins found in living organisms. The specific sequence of amino acids in a polypeptide chain determines how the protein will fold and function.

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5 Must Know Facts For Your Next Test

  1. Polypeptide chains can be made up of 20 different standard amino acids, allowing for countless combinations and unique protein structures.
  2. Peptide bonds are formed through a dehydration synthesis reaction, where water is released as the bond is created.
  3. Polypeptide chains can consist of hundreds to thousands of amino acids, and their length influences the protein's complexity and function.
  4. The order of amino acids in a polypeptide chain is dictated by the genetic code within DNA, which is transcribed into mRNA during protein synthesis.
  5. Post-translational modifications can occur after polypeptide chains are synthesized, altering their structure and function in significant ways.

Review Questions

  • How does the sequence of amino acids in a polypeptide chain affect its overall structure and function?
    • The sequence of amino acids in a polypeptide chain is crucial because it determines how the chain will fold into its final three-dimensional shape. This folding is influenced by interactions between the side chains of the amino acids, such as hydrogen bonding, hydrophobic interactions, and ionic bonds. The specific structure achieved through this folding directly affects the protein's function, including its ability to bind to other molecules or catalyze reactions.
  • Discuss the role of peptide bonds in forming polypeptide chains and how they contribute to protein stability.
    • Peptide bonds link individual amino acids together to form polypeptide chains through dehydration synthesis. This strong covalent bond contributes significantly to the stability of the protein's primary structure. The stability provided by peptide bonds helps maintain the integrity of the protein as it undergoes folding and interacts with other biomolecules, ensuring proper function within biological systems.
  • Evaluate the impact of post-translational modifications on the function of polypeptide chains in proteins.
    • Post-translational modifications can significantly alter the function of polypeptide chains after they are synthesized. These modifications, such as phosphorylation, glycosylation, or ubiquitination, can change the protein's activity, localization, and interactions with other molecules. By modulating these properties, post-translational modifications play a critical role in regulating cellular processes and responding to environmental changes, ultimately affecting how proteins contribute to biological functions.
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