Unit 7.1 Flashcards
What is similar about amino acid structures?
They have an amino and carboxyle group in them.
What is different about amino acid structures?
Their side chains / r-groups. This defines what kind of amino acid they are.
What are the four levels of protein structures?
Primary, Secondary, Teritiary, and Quaternary
What does each protein structure level do?
Primary = sequence of amino acids in a polypeptide chain
Secondary = Folded structures that form within polypeptides. Most common types are a-helix and b pleated sheets
Tertiary = Interactions between side chains so that the proteins fold based on different attractions.
Quaternary = Multiple protein peptide chains connected together
What happens to a protein during denaturation?
Excessive heat or some other major issue breaks some bond or reconfigures, causing the protein to not function correctly.
How is tertiary structure formed by interactions between hydrophobic molecules?
They all turn in toward the center, which twists the strand.
How is tertiary structure formed by interactions between hydrophillic molecules?
All those molecules turn outward toward the water, twisting the strand again.
How is tertiary structure formed by interactions between acidic and basic side chains?
They are attracted to one another due to their opposite charges, so if they are far away from each other on the chain, the whole thing will have to twist a lot.
How is tertiary structure formed by interactions between cysteines?
They are attracted to one another.
Give an example of a protein type and function.
Antibodies = They engage in constant battle in the bloodstream. They fight things that are foreign to the body.
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 have to turn outward toward the water and could possibly pull that whole part of the chain outward.
How are the effects and results of protein denaturation different from the effects and results of a mutation?
A protein can sometimes still function normally with a mutation, because the part that mutated could be very similar to the part it replaced. A denaturation on the other hand just fully destroys the protein from functioning at all.
