Skip to search formSkip to main contentSkip to account menu

Myoglobin

Known as: Myoglobin [Chemical/Ingredient], myoglobins 
A conjugated protein which is the oxygen-transporting pigment of muscle. It is made up of one globin polypeptide chain and one heme group.
National Institutes of Health

Related topics

Related topics

34 relations

Broader (4)

Carrier ProteinsGlobinHemeproteinsMuscle Proteins
In BloodMB geneMyoglobin Ag:PrThr:Pt:Tiss:Ord:Immune stainMyoglobin measurement

Narrower (12)

apomyoglobinbiliverdin-apomyoglobin complexcarboxymyoglobincarboxysulfmyoglobin

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2008
Highly Cited
2008
Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin
Myoglobin is a globular protein involved in oxygen storage and transport. No consensus yet exists on the atomic level mechanism… 
Highly Cited
2000
Highly Cited
2000
The role of cavities in protein dynamics: crystal structure of a photolytic intermediate of a mutant myoglobin.
We determined the structure of the photolytic intermediate of a sperm whale myoglobin (Mb) mutant called Mb-YQR [Leu-(B10)-->Tyr… 
Highly Cited
1995
Highly Cited
1995
Structural and functional effects of apolar mutations of the distal valine in myoglobin.
High-resolution structures of the aquomet, deoxy, and CO forms of Ala68, Ile68, Leu68, and Phe68 sperm whale myoglobins have been… 
Highly Cited
1994
Highly Cited
1994
Ascorbyl free radical: a noninvasive marker of oxidative stress in human open-heart surgery.
Highly Cited
1984
Highly Cited
1984
Reaction of myoglobin with phenylhydrazine: a molecular doorstop.
X-ray crystallographic studies of myoglobin do not show an entrance or exit path for potential ligands from the surface to the… 
Review
1978
Review
1978
Analysis of acid-base properties of peroxidase and myoglobin.
Two heme-linked groups of horseradish peroxidases, characterized by pKa = 5.8 (isoenzyme A) and 7.3 (isoenzyme C), are believed… 
Highly Cited
1975
Highly Cited
1975
Neutron diffraction analysis of myoglobin: structure of the carbon monoxide derivative
The locations of hydrogen and deuterium atoms and water molecules have been investigated in carbon monoxide myoglobin using… 
Highly Cited
1969
Highly Cited
1969
Autoxidation of oxymyoglobins.
Highly Cited
1968
Highly Cited
1968
The transition between 'acid' and 'alkaline' ferric heme proteins.
Highly Cited
1964
Highly Cited
1964
Properties of Components of Myoglobin of the Sperm Whale
RUMEN1 isolated from seal, by chromatography on CM-cellulose in tris buffer at pH 8.5, five myoglobins all with the same iron… 
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy (opens in a new tab), Terms of Service (opens in a new tab), and Dataset License (opens in a new tab)