7.1 Study Guide Flashcards
(9 cards)
What are the four levels of protein structure?
Primary: Determines final shape
Secondary: Hydrogen bonds between carboxyl, a helix and B-Pleated sheet
Tertiary: Final 3-D shape of a single polypeptide
Quaternary: More than one polypeptide bonded together.
What happens during protein denaturation?
Denaturation disrupts the hydrogen and ionic bonds.
What makes amino acids?
Polar= They all have a polar functional group
Acidic=The side chains are negatively charged
Basic= They have positive charges
Nonpolar/Hydrophobic= Made up of Carbon and Hydrogen
How is the tertiary formed by interactions from: Hydrophiobic, acidic and basic, cysteines and hydrophilic
Hydrophobic=Fold told the interior of protein
Acidic and Basic: They attract the positive and negative charge
Cysteines: Form disulfide bridge covalent
Hydrophilic: Form hydrogen bonds/ towards outer portion of protein
Why and how would the structure and function of a protein change if a hydrophobic amino acid was substituted for a hydrophilic one
It would disrupt the proteins folding pattern and the function would be impacted because the introduced polar side would be energetically unfavorable.
How are the effects and results of protein denaturation different from the effect and results of a mutation?
Protein denaturation disrupts a proteins secondary and tertiary structures causing it to lose its functional shape while mutation on disrupts the primary structure.
A protein that breaks down starch into monomers of glucose would belong to which groups of proteins.
Enzymes
Level of protein structure (1,2,3,4)
Not affected by denaturation: 1
Sequence of amino acids: 1
Contains multiple peptide chains: Quaternary
3-D folded shape of polypeptide determined by the side chains of amino acids: 3
Structures at this level are similar throughout proteins: 2
Nonpolar
Only have carbon and hydrogen
