Drag each of the following items into the corresponding boxes to indicate the protein structural level that is predominantly affected by the chemical interactions listed. Some items may be placed in more than one box. Reset Help Hydrogen bonds between polar groups in amino acid side chains Hydrophobic interactions between amino acid side chains lonic bonds between positively- charged and negatively-charged amino acid side chains Peptide bonds Hydrogen bonds between carbonyl oxygens and amino nitrogens within a polypeptide backbone Disulfide bonds Primary structure Seconday structure Tertiary structure Quaternary structure

Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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**Protein Structure and Chemical Interactions**

In this exercise, you are tasked with associating different chemical interactions with the four levels of protein structure: primary, secondary, tertiary, and quaternary. Each interaction type may be associated with more than one structural level.

### Chemical Interactions:

1. **Peptide bonds**
2. **Hydrogen bonds between polar groups in amino acid side chains**
3. **Hydrophobic interactions between amino acid side chains**
4. **Ionic bonds between positively-charged and negatively-charged amino acid side chains**
5. **Disulfide bonds**
6. **Hydrogen bonds between carbonyl oxygens and amino nitrogens within a polypeptide backbone**

### Protein Structural Levels:

- **Primary Structure:** 
  - Defined by the sequence of amino acids in a polypeptide chain linked by peptide bonds.

- **Secondary Structure:** 
  - Characterized by hydrogen bonds between carbonyl oxygens and amino nitrogens within the polypeptide backbone, forming alpha helices and beta sheets.

- **Tertiary Structure:** 
  - Involves various interactions including hydrogen bonds between polar side chains, hydrophobic interactions, ionic bonds, and disulfide bonds, contributing to the three-dimensional folding of a protein.

- **Quaternary Structure:** 
  - Represents the interaction and assembly of multiple polypeptide subunits through similar interactions as the tertiary structure.

Drag and drop each type of interaction into its corresponding structural level(s) based on how these interactions predominantly affect the protein's structure.
Transcribed Image Text:**Protein Structure and Chemical Interactions** In this exercise, you are tasked with associating different chemical interactions with the four levels of protein structure: primary, secondary, tertiary, and quaternary. Each interaction type may be associated with more than one structural level. ### Chemical Interactions: 1. **Peptide bonds** 2. **Hydrogen bonds between polar groups in amino acid side chains** 3. **Hydrophobic interactions between amino acid side chains** 4. **Ionic bonds between positively-charged and negatively-charged amino acid side chains** 5. **Disulfide bonds** 6. **Hydrogen bonds between carbonyl oxygens and amino nitrogens within a polypeptide backbone** ### Protein Structural Levels: - **Primary Structure:** - Defined by the sequence of amino acids in a polypeptide chain linked by peptide bonds. - **Secondary Structure:** - Characterized by hydrogen bonds between carbonyl oxygens and amino nitrogens within the polypeptide backbone, forming alpha helices and beta sheets. - **Tertiary Structure:** - Involves various interactions including hydrogen bonds between polar side chains, hydrophobic interactions, ionic bonds, and disulfide bonds, contributing to the three-dimensional folding of a protein. - **Quaternary Structure:** - Represents the interaction and assembly of multiple polypeptide subunits through similar interactions as the tertiary structure. Drag and drop each type of interaction into its corresponding structural level(s) based on how these interactions predominantly affect the protein's structure.
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