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Ch.10 Proteins Workers of the Cell
Frost - General, Organic and Biological Chemistry 4th Edition
Frost4th EditionGeneral, Organic and Biological ChemistryISBN: 9780134988696Not the one you use?Change textbook
Chapter 6, Problem 71b

Identify the level of protein structure associated with each of the following:
b. hydrogen bonding between backbone atoms

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1
Understand the four levels of protein structure: primary, secondary, tertiary, and quaternary. Each level describes a different aspect of the protein's organization.
Recall that the primary structure refers to the sequence of amino acids in the polypeptide chain, held together by peptide bonds.
Recognize that the secondary structure involves local folding of the polypeptide chain into structures such as alpha-helices and beta-pleated sheets. These structures are stabilized by hydrogen bonding between backbone atoms (specifically, between the carbonyl oxygen of one amino acid and the amide hydrogen of another).
Note that tertiary structure refers to the overall three-dimensional shape of a single polypeptide chain, stabilized by interactions such as hydrogen bonds, ionic bonds, hydrophobic interactions, and disulfide bridges, but these involve side chains rather than backbone atoms.
Conclude that the level of protein structure associated with hydrogen bonding between backbone atoms is the secondary structure.

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Key Concepts

Here are the essential concepts you must grasp in order to answer the question correctly.

Protein Structure Levels

Proteins have four levels of structure: primary, secondary, tertiary, and quaternary. Each level represents a different aspect of protein organization, from the sequence of amino acids (primary) to the overall three-dimensional shape (tertiary) and the assembly of multiple polypeptide chains (quaternary). Understanding these levels is crucial for analyzing protein function and stability.
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Summary of Protein Structure Concept 1

Secondary Structure

The secondary structure of a protein refers to local folded structures that form within a polypeptide due to hydrogen bonding between backbone atoms. Common examples include alpha helices and beta sheets. These structures are essential for the overall stability and functionality of proteins, as they contribute to the protein's three-dimensional conformation.
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Hydrogen Bonding

Hydrogen bonding is a type of weak chemical bond that occurs when a hydrogen atom covalently bonded to an electronegative atom, like oxygen or nitrogen, interacts with another electronegative atom. In proteins, these bonds are critical for stabilizing secondary structures, as they help maintain the shape and integrity of the protein by linking different parts of the polypeptide chain.
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