Levels of protein structure shown by the myoglobin molecule

Amino acid colour codes: ASP, GLU, CYS, MET, LYS, ARG, SER, THR, PHE, TYR, ASN, GLN, GLY, LEU, VAL, ILE , ALA, TRP, HIS and PRO.
PRIMARY STRUCTURE
The myoglobin molecule consists of 151 amino acid residues, in a single chain. Initial ("skinny ball and stick") scheme shows 1336 atoms, coloured by elements, but no hydrogens.
- Name / Number / unlabel amino acid residues
- Colour by amino acids / Colour by elements
- Highlight peptide bonds between amino acids.


SECONDARY STRUCTURE *, **: These options sacrifice detail to emphasise the coiling of the polypeptide chain
Display options:
- Ball and sticks / wireframe / * trace / ** cartoon Colour by structure
- Show / hide hydrogen bonds between main chain peptide groups
- Show prolines at ends of helices

TERTIARY STRUCTURE
- Dots on / off to display molecular surface
- Show haem unit (ball & stick) and histidines 64 & 93
- Show / hide sidechain R group H bonds
- Show acidic and basic/ polar and non-polar sidechains / reset colours

QUATERNARY STRUCTURE
Unlike haemoglobin, myoglobin does not have a quaternary structure, as it consists of a single polypeptide chain.

FUNCTION: OXYGEN STORAGE WITHIN MUSCLE
- Show oxygens
This graphics display was prepared to support a unit on the levels of protein structure using haemoglobin and myoglobin as an example.