Proteins Structure and Function Flashcards
In what level of protein folding does hydrogen bonding occur
Secondary
amino acids are joined by what kind of reaction
dehydration reaction
synthesis of protein occurs from what end of amino acid to what end
starts with amino side on the left and finishes with the carboxyl end on the right side
Describe the planes of peptide bond
- carbon and nitrogen form planes
- rotation can occur around bonds attached to alpha carbon
- side chains alternate above and below chain
- peptide bond is a resonance between two structures
- results in negative charge on oxygen and positive charge on nitrogen
Is the cis or trans configuration favored
Trans because the side chains are bulky and would bump into each other if they were on the same side of the chain
which amino acid cannot be in alpha helix
Proline due to its rigid structure, if inserted it would end the alpha helix
describe the bonding of an alpha helix
oxygen atom of a carbonyl binds to a hydrogen through hydrogen binding that is attached to a nitrogen 4 amino acids down in the chain.
describe how our body deals with proline in a protein structure
it can enzymatically switch it from trans to cis or vice versa to get it to fit into the growing peptide chain,
where are r groups positioned in helix
on the outside of the peptide so it can interact with other r groups or external environment
parallel and antiparallel beta pleated sheets
parallel means the amino terminus and carboxyl terminus are running in the same direction as far as the planes whereas antiparallel means they are running in the opposite plane or direction
What 3 bonds hold the secondary structures together to help form tertiary structures
hydrogen bonds, hydrophobic interactions, and ionic bonds
What type of bonds are in tertiary structure
sulfhydryl (S-S) bonds which are a type of covalent bond