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Questions and Answers
What is the characteristic shape of globular proteins?
What is the characteristic shape of globular proteins?
What is the primary structure of a protein?
What is the primary structure of a protein?
What is the result of regular folding of the backbone of the polypeptide chain due to hydrogen bonding?
What is the result of regular folding of the backbone of the polypeptide chain due to hydrogen bonding?
What is the type of bond responsible for the secondary structure of proteins?
What is the type of bond responsible for the secondary structure of proteins?
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What is the name of the structure that resembles the pleated folds of drapery?
What is the name of the structure that resembles the pleated folds of drapery?
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What is the consequence of a change in the primary structure of a protein?
What is the consequence of a change in the primary structure of a protein?
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What is the level of protein structure that refers to the shape of a single polypeptide chain?
What is the level of protein structure that refers to the shape of a single polypeptide chain?
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How many levels of protein structure are there?
How many levels of protein structure are there?
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Study Notes
Protein Structure
- Globular proteins have a spherical shape and are usually soluble in water, with examples being insulin and albumins.
Levels of Protein Structure
- There are four levels of protein structure: primary, secondary, tertiary, and quaternary, with each level being more complex than the previous one.
Primary Structure
- The primary structure of a protein refers to the specific sequence of amino acids in a polypeptide chain.
- A protein can have one or more polypeptide chains.
- Any change in the primary structure (i.e., the sequence of amino acids) creates a different protein.
Secondary Structure
- The secondary structure of a protein refers to the shape of a long polypeptide chain.
- There are two types of secondary structures: α-helix and β-pleated sheet structure.
- These structures arise due to the regular folding of the polypeptide chain backbone due to hydrogen bonding between –NH– and –C=O groups of the peptide bond.
- α-Helix is a common way in which a polypeptide chain forms all possible hydrogen bonds by twisting into a right-handed screw (helix) with the –NH group of each amino acid residue hydrogen bonded to the –C=O of an adjacent turn of the helix.
- β-Pleated sheet structure involves peptide chains stretched out to nearly maximum extension and laid side by side, held together by intermolecular hydrogen bonds, resembling the pleated folds of drapery.
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Description
This quiz covers the different levels of protein structure, including primary, secondary, tertiary, and quaternary structures. Learn about the characteristics of globular proteins and more!
