Lecture 5 Part 2 Protein Structure and Function Flashcards
What is the primary structure of a protein?
The linear sequence of amino acids.
What are the major types of secondary structures?
⍺-helix, β-strands, and β-turns.
What is tertiary structure?
The 3D folding of secondary structures into a stable shape.
What is quaternary structure?
The assembly of multiple polypeptides into a larger functional protein.
How does the amino acid sequence affect protein structure and function?
It determines how the protein folds, which influences its function.
What role do disulphide bonds and non-covalent interactions play in protein structure?
They stabilize the protein’s shape.
Why is flexibility important in protein structure?
Proteins need to change shape to perform functions, like enzymes during reactions.
What can happen if a protein misfolds?
It can cause diseases like Alzheimer’s or prion diseases.
What is the difference between PrPC and PrPSC?
PrPC is the normal prion protein, and PrPSC is the misfolded, disease-causing version.
What interactions stabilize tertiary and quaternary structures?
Non-covalent forces and disulfide bonds.
How does a single amino acid change cause sickle-cell anemia?
Glutamate is replaced by Valine, causing hemoglobin to stick together and deform red blood cells.
How is protein structure useful in drug design?
It helps design inhibitors that can block protein function or interactions.
what happens when PrPSc interacts with PrPc?
it can change the structure of the original prion protein further spreading the disease
