Secondary Structure – Peptides
About the Lecture
The lecture Secondary Structure – Peptides by Kevin Ahern, PhD is from the course Biochemistry: Basics.
Included Quiz Questions
Which of the four levels of protein organization has a regular repeating structure arising from interactions of nearby amino acids?
- Secondary
- Primary
- Tertiary
- Quaternary
What are the main forces that were described as stabilizing secondary structure?
- Hydrogen bonds
- Covalent bonds
- Disulfide bonds
- Ionic bonds
- Carbon-carbon bonds
What do the protein structures of collagen, keratin, and fibroin (the protein of silk) have in common?
- They do not have a tertiary structure.
- Their structures cannot be predicted from their primary amino acid sequences.
- Hydrogen bonds between carboxyl groups help stabilize their structures above the primary level.
- Their alpha-helix and beta-strand sequences have the same proportions of amino acids.
- Their structures may show forward and reverse turns.
Which of the following amino acids have a high propensity for reverse turns?
- Glycine
- Alanine
- Glutamic acid
- Valine
- Isoleucine
Which of the following statement is FALSE regarding the secondary structure of proteins?
- There are 4 structures used to describe the secondary structure of proteins.
- Alpha helixes and beta-strands were discovered by Linus Pauling.
- In alpha-helixes, hydrogen bonds are formed between carboxyl oxygen and the amine hydrogen.
- Beta-sheets are groups of beta-strands from different parts of a protein.
- Proline and glycine are frequently found in reverse turns.
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Author of lecture Secondary Structure – Peptides
Kevin Ahern, PhD
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I understand very well, thank you Professor Kevin, these help me a lot
My name is Barbara, I'm from Colombia and I really like your videos Mr. Kevin, because I think the content is easy to understand.
