A protein in which at least one polypeptide chain is folded in a three-dimensional configuration. Globular proteins have a variety of functions (e.g. acting as enzymes, facilitating transport, and providing storage).

Unlike fibrous proteins which only play a structural function, globular proteins can act as: Enzymes, by catalyzing organic reactions taking place in the organism in mild conditions and with a great specificity. Different esterases fulfill this role.

Globular proteins have multiple functions as they are used to form enzymes, cellular messengers, amino acids but fibrous proteins act only as structural proteins. Globular proteins are highly branched or coiled structures and are majorly responsible for transportation of vital nutrients like oxygen through hemoglobin.

Fibrous proteins are generally composed of long and narrow strands and have a structural role (they are something) Globular proteins generally have a more compact and rounded shape and have functional roles (they do something)

The example of globular protein is haemoglobin which is considered as the member of the globin protein family. The other globulins are alpha beta and gamma ( IgA, IgD, IgE, IgE and IgM.) The signal transduction proteins and enzymes with their metabolic functions are globular in shape.

1) Globular protein: Globular proteins are spherical in shape and soluble in water, acids, bases, neutral salt solution or alcohol. Example is hemoglobin. a) Hemoglobin: Hemoglobin is represented as Hb; it is a protein molecule which is present in (RBCs) red blood cells.

hemoglobin
Among the most known globular proteins is hemoglobin, a member of the globin protein family. Other globular proteins are the immunoglobulins (IgA, IgD, IgE, IgG and IgM), and alpha, beta and gamma globulins. See protein electrophoresis for more information on the different globulins.

-Globular proteins are pretty highly branched or termed as coiled structures. -Globular proteins are highly made up of not just primary, secondary but also the tertiary and in many cases occasionally quaternary structures. -Hemoglobin is an well explained example of globular protein.

Globular proteins are compact, roughly spherical (circular) in shape and soluble in water. Globular proteins form a spherical shape when folding into their tertiary structure because: their non-polar hydrophobic R groups are orientated towards the centre of the protein away from the aqueous surroundings and.

In particular, glycoproteins in the cell membrane are very important for cell-to-cell recognition and adhesion, as well as serving as receptors for other types of molecules.

On the other hand, the strength of attraction that exists between the globular proteins has weak hydrogen bonding. The primary type of fibrous proteins includes silk, wool, and skin. On the other hand, the main types of globular proteins include egg, milk , and others. Advertisement – Continue Reading Below

Proteomics. Globular proteins tend to a single specific conformational structure.

Transport proteins, such as globular proteins, transport molecules across cell membranes through facilitated diffusion . Glycoproteins have a carbohydrate chain attached to them. They are embedded in the cell membrane and help in cell to cell communications and molecule transport across the membrane.

Difference Between Fibrous and Globular Protein Definition. A fibrous protein refers to a class of insoluble proteins which constitute the main structural elements of the body while a globular protein refers to a protein soluble in Shape. Structure. Amino Acid Sequence. Intermolecular Interactions. Solubility in Water. Durability. Function. Examples. Conclusion.