Lecture 4: Proteins and Nucleic Acids Flashcards
What occurs during the tertiary folding structure?
- Folding includes side chains
- Can result in a fully functional protein
-Formed by a bunch of low energy interactions
-This is still a monomer
List the interactions that occur during the tertiary step of protein folding(5)
- Hydrogen bonds between side chain and carbonyl group
- Hydrogen bonds between two side chains
- Hydrophobic interactions + van der waals interactions between uncharged side chains
- Disulfide bonds between cysteines(amino acid)
- Ionic bond between the amino and carboxyl group
How is the disulphide bond/bridge created during folding?
Cysteines have a sulfide group, during the folding to get the tertiary structure the cysteines come close together even if they have many amino acids between them and they then form a disulfide bond
-The disulfide bond is the only covalent bond that forms outside of the peptide bond and the only covalent bond between two amino acids
Hydrophobic interactions during tertiary folding
-Stretches of hydrophobic amino acids will rearrange away from water(minimizes disruption of hydrogen network)
-All the hydrophilic amino acids will rearrange to interact with water, they will be on the outside
What’s the major force of protein folding?
Hydrophobic interactions
What happens during the quaternary structure?
-Some proteins are not yet functional after the tertiary folding, so they must undergo another step of folding to become a quaternary structure
-In the quaternary stage proteins have to form either a dimer or tetramer
Dimer vs Tetramer
Dimer: Combination of two polypeptides
Tetramer: Combination of four polypeptides
Consequences of increased temperature on protein
- Increased temperature can cause proteins to denature
Consequences of mutations
Mutate a single amino acid in a polypeptide chain can partially or sometimes completely destroy protein function or it can do nothing at all
How would you prove that proteins carry everything needed for folding in their primary sequence?
- Heat up the ribonuclease(protein) to 80 degrees.
- At 80 the protein will denature.
- Bring the protein back down to 20 degrees, if it refolds at 20 degrees this proves that the primary sequence contains everything needed for folding
What is protein turnover?
-Half-life
-Breakdown of protein into amino acids and then resynthesis of proteins
-Break down of old useless proteins to then make more new ones
-Occurs constantly in cells
What are chaperones?
-Specialized proteins that help keep other proteins from interacting inappropriately with another.
-They keep proteins separated from each other until they mature and individually fold and then they are released
Basic Structure of Nucleotides
- Nitrogenous Base
- Backbone made up of sugar
- Phosphate group
What are the sugars found in DNA and RNA?
DNA: Deoxyribose (H)
RNA: Ribose (OH)
What carbons are used in the elongation of DNA and RNA?
Carbons 3 prime and 5 prime