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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

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12y ago
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11y ago

The primary structure of hemoglobin is the same as any other protein. It is a chain of amino acids arranged in a chain linked by peptide bonds. It then undergoes secondary, tertiary, and quaternary folding.

Adult, human hemoglobin has four components: 2-alpha and 2-beta subunits which surround an iron ion.

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15y ago

Hemoglobin occupies the fourth or quaternary level of protein structure. I believe that this is due in part to the addition of the "heme" or iron component of the protein.

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13y ago

quaternary, due to the 4 haem groups; 2 alpha chains and 2 beta chains.

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13y ago

because it has 4 haem groups

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11y ago

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Q: Hemoglobin structure is tertiary or quaternary?
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Related questions

Is hemoglobin a protein that exhibits the quaternary structure of protein folding?

The tertiary structure is the folding


A fully functional molecule of hemoglobin is what kind of protein structure?

The structure of the hemoglobin in a molecule is the quaternary structure.


Quaternary structure of proteins?

The quaternary structure is the overall structure of an enzyme complex. This is made of at least two separate polypeptide chains. The 3D structure of one polypeptide is known as the tertiary structure.


Name an example of a protein structure with quaternary structure using this protein as an example determine its primarysecondary and tertiary structure interraction and factors involved in the conform?

Hemoglobin.


What the difference between tertiary and quatarnary?

The Tertiary Period and Quaternary Period are divisions of geologic time. The Tertiary Period occurred first, from 65.5 to 2.6 million years ago, and covers the time period from the extinction of the dinosaurs to the beginning of the Ice Ages. The Quaternary Period occurred from 2,588,000 years ago until today, beginning when glaciation started.


What are the four levels of protein structure?

primary, secondary, tertiary, and quaternary


Is collagen a secondary or tertiary structure?

With most proteins, it has a secondary and tertiary structure.


Differentiate the four types of protein structure?

There are four types of protein structure. These include primary structure, secondary structure, tertiary structure, and quaternary structure. Primary structure is the amino acid sequence. Secondary structure is the shape of the molecule. Tertiary structure is the interaction between groups. Quaternary structure is the interactions between protein subunits.


What is a tertiary protein structure exemplified by?

Hemoglobin - formed with alpha helices and/or beta sheets, but as one, contiguous polypeptide. Superoxide dismutase would be a good example of a quaternary structure protein, since it is made of more than one polypeptide chain.


Proteins with more than one polypeptide chain have what structure?

These have quaternary structure. This is the overall shape of all the chains combined. The 3D shape of one polypeptide chain is the tertiary structure.


The association of four subunit peptides in a fully functional molecule of hemoglobin is a good example of?

The quaternary structure of proteins.


What bonds do Tertiary and quaternary structure of proteins involve?

Several, and they are mostly the same as tertiary structure. Hydrogen bonding, London dispersion/Van der Waal's forces, dipole moments, disulfide bonds, and occasionally (such as in hemoglobin), ionic bonding.