3.3 Proteins Flashcards
What are the four levels of protein structure?
1, 2, 3, and 4 degrees
What is the 1 degree of protein structure?
primary structure
What is the 2 degree of protein structure?
secondary structure
What is the 3 degree of protein structure?
tertiary structure
What is the 4 degree of protein structure?
quaternary structure
What happens during protein denaturation?
this is the unfolding of a protein that destroys functionality, they disrupt hydrogen and ionic bonds. some can return back to their original structure but most of the time they cannot
How is tertiary structure formed by hydrophobic interactions?
hydrophobic groups cluster together on the inside of the protein leaving hydrophilic amino acids on the outside to interact with surrounding water molecules
How is tertiary structure formed by hydrophilic interactions?
it is stabilized by the outside polar hydrophilic hydrogen and ionic bond interactions
How is tertiary structure formed by acidic and basic side chains?
the particular proteins determine its tertiary structure
How is tertiary structure formed by cysteine side chains?
they act like molecular safety pins, keeping parts of the polypeptide firmly attached to one another
Why and how would the structure and function of a protein change if a hydrophobic amino acid was substituted for a hydrophilic one?
The structure would change because the protein would not be able to bend and go into the correct shape it needs to. If the structure changes, then it won’t be able to carry out its proper function, it won’t be able to do anything.