2.3 - Hierarchy of Protein Structure Flashcards
primary structure
amino acid chain
what defines the secondary structure of a protein? (2)
- phi and psi angles (backbone torsion angles) of backbone atoms of amino acid residues
- hydrogen bonds between main chain atoms
units of secondary structure (2)
- alpha-helix
- beta-strand
a-helix (2)
- main chain N and O atoms H-bonded to one another
- R groups stick out from a-helix influencing higher level of protein organisation
amino acids that are food a-helix formers (4)
- Ala
- Glu
- Leu
- Met
amino acids that are poor a-helix formers (3)
- Pro
- Gly
- Tyr
B-strand (3)
- series of B-strands H-bonded form B-pleated sheets
- R-groups point alternately up and down
- B-strands can be parallel or antiparallel
secondary structure breakers
many amino acids have side chains which disrupt secondary structure
examples of secondary structure breakers (3)
- Gly side chain linked to alpha N, no N-H to H-bond (rigid structure due to ring restricts Phi angle)
- Pro H-bonding side chains compete with backbone H-bonds
- Asp, Asn, Ser clusters of breakers, leads to regions (loops/turns) which mark boundaries of secondary structure, link secondary structure segments
Beta-turn (2)
- H-bond between carbonyl O and amide H of residue 3 positions down
- forces reverse of direction chain
mixed B-strands (2)
- 20% B-sheets of known proteins mix parallel and antiparallel sheets
- almost all B-sheets (parallel, antiparallel, mixed) have twisted strands, always right-handed twist
B-propeller topology (2)
- bends and turns connect units of secondary structure
- protein structures also have “loops”
supersecondary structures (motifs) (2)
- arrangement of 2/3 consecutive secondary structures in specific arrangement
- some have specific functions e.g. DNA binding
greek key motif in antiparallel B-sheets (2)
- 2 antiparallel B-strands pair up first, loops in middle, then strands 1 and 2 form H-bonds
- occur very often, frequently found in structures with 2 antiparallel B-sheets
B-a-B motif
occurs in almost all proteins with parallel B-sheets
B-a-B motif form
right handed connection, via right handed a-helix (all B-a-B motifs connected this way)
tertiary structure (3)
- secondary structure elements associate to form 3D structure
- single polypeptide chain
- repeating motifs
quaternary structure
association of 2/more polypeptide chains