Hemoglobin-1 Flashcards
Give 2 examples of secondary protein structure
Alpha helix and Beta-sheet
Describe the alpha-helix structure of secondary protein structure
Helix is stabilized by hydrogen bonding
- Hydrogen bonds occur between the atoms that participate in the peptide bond
- So “repetitive hydrogen” bonding
- Every 4th peptide bond interacts with each other
- amino acid side chains stick out to the side of the helix
Describe the B-sheet of secondary protein structure
Stabilized by hydrogen bonding
-Involves the atoms that participate in the peptide bond
- Repetitive hydrogen bonding
Amino acid side chains stick out above and below the plane of the sheet
Describe a quarter nary structure if a protein
Two or more polypeptides that associate together to carry out some function
Describe a tertiary structure of a protein
Regions of secondary structures fold on themselves to form a tertiary structure
Give an example of a fibrous protein and why it is as such
Collagen is a fibrous protein
A tightly wound triple hekix(not alpha helix)
Collagen has a repetitive structure :
- every 3 amino acid is glycine - Helps with tight packing
What are the characteristics of globular proteins?
- Polar amino acid side chains on surface(adds to solubility)
- Nonpolar amino acid side chains in the interior hydrophobic core)
- some sort of metabolic function: catalytic, transport etc.
- Variety/combo os secondary structure type: B-sheet, a-helix, turn
Most globular proteins are a combination of ….
Alpha helix and beta-sheet linked by turns (or beta bends)
What is a prosthetic group?
A non-protein component found on some proteins
For hemoglobin, heme is the prosthetic group
Differentiate the common oxidation states of iron
Ferrous state- 2+ Fe
Ferric state- 3+
How does ferrous iron play a role in holding oxygen in hemoglobin?
Fe2+ can form 6 bonds 4 covalent coordinate bonds to nitrogens
Histidine in hemoglobin binds to the iron
The last binding site on iron forms a reversible bond to oxygen