Last modified on 8 January 2013, at 06:18  Structural
Biochemistry/Myoglobin  Characteristics of myoglobinEdit
Myoglobin is a relatively small protein of mass 17.8kDa made up
of 153 amino acids in a single polypeptide chain. It was the
first protein to have its three-dimensional structure determined
by x-ray crystallography by John Kendrew in 1957. Myoglobin is a
typical globular protein in that it is a highly folded compact
structure with most of the hydrophobic amino acid residues
buried in the interior and many of the polar residues on the
surface. X-ray crystallography revealed that the single
polypeptide chain of myoglobin consist entirely of alpha-helical
secondary structure. In fact there are eight alpha-helical
secondary structure in myoglobin. Within a hydrophobic cervice
formed by the folding of the polypeptide chain is the heme
prosthetic group. This nonpolypeptide unit is noncovalently
bound to myoglobin and is essential for the biological activity
of the protein. Myoglobin is a small oxygen-bind