1/13
Looks like no tags are added yet.
Name | Mastery | Learn | Test | Matching | Spaced | Call with Kai |
|---|
No analytics yet
Send a link to your students to track their progress
What are the basic components of an amino acid structure?
Central α-carbon, amino group (-NH₂), carboxyl group (-COOH), hydrogen atom, and variable side chain (R-group).
Define peptide bond formation.
A condensation reaction where the amino group of one amino acid reacts with the carboxyl group of another, releasing water.
What defines the primary structure of a protein?
The linear sequence of amino acids in a polypeptide chain.
What is an example of a protein that features specific disulfide bridges?
Insulin, which has two inter-chain and one intra-chain disulfide bridge.
Identify the two main types of secondary structures in proteins.
α-Helix and β-Sheets.
What stabilizes the α-helix structure in proteins?
Hydrogen bonds between carbonyl oxygen and amide hydrogen.
What is the overall 3D arrangement of a protein known as?
Tertiary structure.
What type of interactions stabilize a protein's tertiary structure?
Hydrophobic interactions, hydrogen bonds, ionic bonds, and disulfide bridges.
How is quaternary structure defined in proteins?
The association of multiple polypeptide chains into a functional protein.
What is the role of glutathione in biological systems?
It acts as an antioxidant, protecting cells from oxidative stress.
What is the configuration of the structural protein collagen?
A triple helix providing tensile strength to connective tissues.
Explain the effects of denaturation on proteins.
Loss of secondary, tertiary, or quaternary structure, disrupting functional capabilities.
What experimental method provides atomic-level resolution of protein structure?
X-ray Crystallography.
What significance do peptides and proteins hold in drug development?
They are crucial for drug discovery, such as insulin for diabetes treatment and monoclonal antibodies for cancer therapy.