Levels Of Protein Structure Flashcards
How is tangling avoided in protein structure, what is this done by?
To avoid tangling parts of chain are stabilised or pleated as they’re made. Held in place by H-bonds. The amount of coiling/pleating depends on primary structure.
What is primary structure?
Sequence of amino acids which form a protein.
What is secondary structure?
Coils to form an alpha helix/beta pleated sheet. H-bonds in place (36 amino acids per 10 coils in alpha-helix).
What is tertiary structure?
Coils/pleats coil or fold. Tertiary structure is vital to function (held in place by bonds/interactions).
What are disulphide bonds?
Amino acid cysteine contains sulphur. Two cysteines close together form a covalent bond.
What are ionic bonds?
Ionic bonds - R-groups may carry a charge, then two amino acids may form an ionic bond.
What are hydrogen bonds?
Hydrogen bonds - Slightly positively charged groups and slightly negatively charged groups, H-bonds form.
What are Hydrophobic/Hydrophilic interactions?
Hydrophilic amino acids need go be on outside of globular proteins.
What does heating a molecule do?
Heating a molecule increases the kinetic energy in the molecule, vibrates wreaking tertiary bonds. This is the process of denaturation as bonds are weak - doesn’t reform if cooled.
What do globular proteins do?
Globular proteins tend to roll up into a compact globe or ball shape structure - water soluble, as water molecules cluster around water soluble R-groups.
What do fibrous proteins do?
Fibrous proteins, typically have regular repetitive sequences of amino acids - usually insoluble in water.
