Myoglobin: Difference between revisions

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Myoglobin is a compact globular protein consisting of just 153 amino acids. The single polypeptide is found in muscles and provides vital stores of  oxygen to the muscle cells when required. Myoglobin, like haemoglobin,, binds to oxygen through its iron containing haem group. It is primarily this iron which gives muscle its red colour. The alpha helical 3D structure of the protein was one of the first to be discovered by John Kendrew who studied myoglobin in sperm whales using x-ray crystallography.
Myoglobin is a compact globular protein consisting of just 153 [[Amino_acids|amino acids]]. The single polypeptide is found in [[Muscle|muscles]] and provides vital stores of [[Oxygen|oxygen]] to the muscle cells when required. Myoglobin, like [[Haemoglobin|haemoglobin]], binds to [[Oxygen|oxygen]] through its iron containing haem group. It is primarily this iron which gives muscle its red colour. The [[Alpha-helix|alpha helical]] 3D structure of the protein was one of the first to be discovered by John Kendrew who studied myoglobin in sperm whales using [[X-ray crystallography|x-ray crystallography]].

Revision as of 20:21, 3 January 2011

Myoglobin is a compact globular protein consisting of just 153 amino acids. The single polypeptide is found in muscles and provides vital stores of oxygen to the muscle cells when required. Myoglobin, like haemoglobin, binds to oxygen through its iron containing haem group. It is primarily this iron which gives muscle its red colour. The alpha helical 3D structure of the protein was one of the first to be discovered by John Kendrew who studied myoglobin in sperm whales using x-ray crystallography.