Protein Structures: Globular and Fibrous Proteins (A-level Biology)

Protein Structures: Globular and Fibrous Proteins

Within the different levels of protein structures, there are different subtypes of proteins. We can classify most 3D proteins (i.e. proteins with tertiary and quaternary structures) into globular and fibrous proteins.

Globular Proteins

Structure of Globular Proteins

  • Globular proteins are round structures. Like their name, globular proteins have a round, spherical formation. This is because the hydrophobic parts of the protein fold inwards while the hydrophilic parts become arranged around the external surface.
  • Globular proteins are water soluble. As only the hydrophilic components of the protein are on the outer surface, globular proteins are soluble in water.

Function of Globular Proteins

Due to their round shape and soluble nature, globular proteins play a wide variety of vital metabolic roles in the human body. The following types of proteins are usually globular proteins:

  1. Enzymes. All enzymes are globular proteins as their round shape can be altered appropriately to fit their target sites with high specificity. Examples include digestive enzymes such as amylase, pepsin, and lipase which break down starch, protein, and fats respectively. 
  2. Transport proteins. Due to their soluble nature, globular proteins function well as transport proteins as they can cross cell membranes. An example is haemoglobin, which transports oxygen.
  3. Messengers proteins. Their solubility also makes globular proteins suitable as messenger proteins, otherwise known as hormones. They regulate the body’s metabolic processes. An example would be insulin, which regulates blood sugar levels.

Example globular protein: Haemoglobin

  • Haemoglobin is made up of 4 globular subunits. Haemoglobin is a quaternary protein, made up of 4 tertiary globular subunits. Two of these subunits consist of α chains, while the other two contains β chains.
  • Each of these globular subunit is linked to haem. Each globular unit is covalently bonded to haem. Haem is not a protein, therefore it is called a “prosthetic group”. Haem contains iron, which oxygen binds to.
  • Haemoglobin is considered a “conjugated protein”. As haemoglobin is a protein that is associated with non-protein structures, it is called a conjugated protein.

Fibrous Proteins

Structure of Fibrous Proteins

  • Fibrous proteins are long chains. They are made up of repeated amino acid sequences that form long polypeptide chains. These chains twist together to form fibrous proteins.
  • Fibrous proteins are water insoluble. As the hydrophobic parts of the polypeptide chains are not folded away from the external environment, fibrous proteins are not soluble in water.

Function of Fibrous Proteins

  • Structural proteins are usually fibrous proteins. As fibrous proteins are stable and insoluble structures, they are not suitable to function as metabolic proteins. Rather, they act well as structural proteins which support and protect tissues. Examples include keratin which provide structure to hair and nails, and collagen, a type of connective tissue in the body.

Example fibrous protein: Collagen

  • Collagen is a strong protein due to the types of bonds in its structure. The proteins in collagen are joined together by hydrogen and covalent bonding,  both of which are extremely strong and stable bonds.
  • Collagen fibres provide support and tensile strength to many structures. Collagen is present in the body as fibres, which consist of many collagen fibrils folded around each other. There are many different types of collagen, and they can be found virtually everywhere in the body, including skin, muscles, tendons and bones.
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FAQs

→What are globular and fibrous proteins?

Globular proteins are proteins that have a compact, spherical shape. They are usually soluble in water and play important roles in cellular processes such as enzymes, hormones, and antibodies. Fibrous proteins are long, thin proteins that are insoluble in water and provide structural support in tissues such as hair, nails, and tendons.

→Why is it called a globular protein?

A globular protein is called so because of its spherical or globular shape. The term “globular” refers to the overall shape of the protein, which is roughly spherical, and the term “protein” refers to the fact that it is a biomolecule made up of amino acids.

The three-dimensional structure of a globular protein is usually highly folded and compact, with the hydrophobic amino acid residues on the inside and the hydrophilic amino acid residues on the outside. This compact and folded structure is stabilized by a combination of hydrogen bonds, ionic bonds, disulfide bonds, and other types of non-covalent interactions.

Globular proteins are typically water-soluble and play many important roles in the body, such as enzymes, transport proteins, and hormones. The spherical shape of globular proteins is also important in their function, as it allows them to interact with other biomolecules in a specific and controlled manner.

→What is the difference between globular protein and fibrous protein?

The main difference between globular proteins and fibrous proteins is their overall shape and function.

Shape: Globular proteins have a roughly spherical or globular shape, while fibrous proteins have an elongated or fibrous shape.

Function: Globular proteins are typically water-soluble and perform a wide variety of functions in the body, such as enzymes, transport proteins, and hormones. Fibrous proteins, on the other hand, are typically insoluble in water and have a more structural role in the body, such as providing support and strength to tissues and organs.

Amino acid sequence: The amino acid sequence of globular proteins is usually irregular, with regions of alpha-helix and beta-sheet secondary structure interspersed throughout the protein. Fibrous proteins, on the other hand, have a more regular amino acid sequence, with long stretches of alpha-helix or beta-sheet secondary structure.

Solubility: Globular proteins are typically water-soluble due to their polar and charged amino acid residues on the surface of the protein, while fibrous proteins are typically insoluble in water due to their non-polar amino acid residues.

In summary, while both globular and fibrous proteins are important biomolecules with specific functions in the body, their shape, amino acid sequence, solubility, and function are different.

→How does the structure of globular proteins affect their function?

The compact, spherical shape of globular proteins allows them to easily bind with other molecules and perform specific functions, such as catalyzing reactions in enzymes, transmitting signals in hormones, or recognizing and neutralizing foreign invaders in antibodies.

→How does the structure of fibrous proteins affect their function?

The long, linear structure of fibrous proteins allows them to provide strength and stability in tissues, as well as forming networks to help maintain the structure of cells and tissues.

→What are some common examples of globular proteins?

Common examples of globular proteins include enzymes, such as lactase and catalase, hormones, such as insulin and testosterone, and antibodies, such as immunoglobulin G.

→What are some common examples of fibrous proteins?

Common examples of fibrous proteins include keratin in hair and nails, collagen in skin and connective tissues, and elastin in elastic tissues.

→How do globular and fibrous proteins differ in their interactions with other molecules?

Globular proteins can interact with other molecules by binding with them through specific, non-covalent bonds. Fibrous proteins generally do not interact with other molecules in the same way as globular proteins, as they do not have the same level of complexity and diversity in their structures.

→How do changes in temperature or pH affect the structure of globular and fibrous proteins?

Changes in temperature or pH can cause structural changes in both globular and fibrous proteins, disrupting their function and stability. For example, elevated temperatures can cause denaturation of proteins, leading to the loss of their native structure and function.

→How important are globular and fibrous proteins in biology?

Globular and fibrous proteins play crucial roles in cellular processes, including metabolism, signaling, and structural support. Understanding their structures and functions is essential for understanding many aspects of biology, from human physiology to the workings of cells and tissues.

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