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Yes. Hemoglobin consists of four heme groups as well as a globin. Globin is a type of protein - proteins are made of polypeptide chains.
A hemoglobin mode is composed of protein known as globin and four hemo groups associated with an iron atom in the lungs.
Hemoglobin is a complex protein with iron groups inside it that bind to oxygen.
Hemoglobin refers to a red protein responsible for transporting oxygen in the blood of vertebrates. The part of the hemoglobin molecule that carbon attaches to is the heme molecule.
yesNo it is a lipid. It has long hydro carbon chains with alcohol groups
The first level
Hemoglobin is a protein that contains an iron ion and assists in transporting oxygen in red blood cells. Hemoglobin also helps to transport carbon dioxide and nitric oxide.
No, proteins are made of amino acid chains, some of which may be modified with attached phosphate groups.
positively charged due to amino groups of its protein tail,the globin.But the medium is negatively charged.
Hemoglobin is made up of four "monomeric subunits" each of which is known as a polypeptide and about the size of many normal individual proteins. Each of these subunits has its own tertiary structure and is about the size of another similar globular protein called Myoglobin. Quarternary structures ONLY exist in proteins with subunits, which are essentially four protein "parts" that are joined together (in this case with Hydrophobic and Ionic interactions) once they are already folded (tertiary structure). 4+ structure is how they fit together. So Myoglobin, with only one subunit does not have a quarternary structure, but does have primary, secondary and tertiary. Insulin, for example has two subunits and it too will have a quarternary structure, or how both subunits fit together
Hemoglobin is a molecule which is consist of 4 HEM groups and a protein named globin. Major duity of hemoglobin is to transfer CO2 and O2 between the tissues and the blood, but those are not the only molecules that can bind to hemoglobin. CO and some other molecules can too and when that happens O2 saturation may go severely down.
Is the many foldings and twists resulting from the interactions of the R group side chains; hydrophobic interactions, hydrogen bonding between polar groups, ionic bonding between charged groups, hydrophyllic interactions and covalent bonding between sulfur containing groups. All this contributes to the globular or other shape the mature protein will take.