The overall shape of myoglobin is approximately disc-shaped. More specifically, it resembles a flattened sphere, with a diameter roughly twice its thickness.
Myoglobin's structure is crucial to its function as an oxygen-storage protein in muscle tissue. While its precise dimensions can vary slightly, the general disc-like form is a defining characteristic. The protein's fold, particularly the hydrophobic core, is highly conserved, contributing to the stability of the molecule. Sequence variations primarily occur on the surface of the protein, allowing for adaptations without disrupting the core structure and function.
