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.
Click on the interactive links in the text below.

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

This molecule can be moved by holding down the left mouse button and dragging. The right button gives many options.
Start .. stop rotation
Click on the interactive links in the text below.
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
DISPLAY
- Start /stop rotation

This graphics display was prepared to support a unit on the levels of protein structure using haemoglobin and myoglobin as an example.

Possibly relevant
material available online
(from Amazon.com)

Possibly relevant
material available online
(from Amazon.co.uk)