Proteins - Lecture Five Flashcards
Elements of Protein Structure
Primary structure
Amino acid sequence of a protein
Secondary structure
3D arrangement of a protein chain over a short stretch of adjacent amino acid residues
Alpha helix and beta-strands/sheet
Tertiary structure
3D structure of a complete protein chain
Quaternary structure
Interchain packing and structure for a protein that contains multiple protein chains
Why are proteins mostly globular?
So the main chain has a double back to form a more compact shape
What are the main chain atoms in a protein
Carbon, nitrogen and calcium
Phi angle
Rotation angle around the N-Ca bond
Psi angle
Rotation angle around the Ca-C’ bond
Phi angle restriction
Can lead to O-O collisions
Psi angle restriction
Can lead to NH-NH collisions
Steric hinderance in Phi-Psi restrictions
Between the hydrogen on the amide nitrogen and the carbonyl oxygen
Alpha Helix key properties
3.6 residue/turn, 5.4Å/turn
Spiral is right handed
Side chains point out from the helix axis
Dipole
Phi angle (Φ) = ~57˚
Psi angle (ψ) = ~47˚
Some residues are ‘helix breakers’ e.g. glycine and proline
Beta structure
Involves adjacent peptide chains, called beta strands, that have an extended standard that allows for hydrogen bonding between chains
One beta-sheet =
Two beta-strand
Average beta-strand length
~6 amino acid residues and can have up to 15 residues