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3.5:

Globular and Fibrous Proteins

JoVE Core
Molecular Biology
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JoVE Core Molecular Biology
Globular and Fibrous Proteins

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Proteins have evolved to form quaternary structures and multi-unit complexes when larger molecules are needed by the cell, rather than having longer amino acid chains. Most proteins fall into one of two categories: globular and fibrous. Globular proteins are compact, with their amino acid chain wound into a spheroid shape. Their secondary structures are usually a mixture of alpha-helices and beta-sheets.   Most intracellular proteins are globular and water-soluble, such as many enzymes and transcription factors. In these structures, the hydrophobic amino acids pack tightly into the middle of the spheroid structure, while the hydrophilic amino acids are found on the outer surface.  Globular proteins interact with each other in a variety of configurations, forming different types of structures including filaments or multimeric complexes. Many form quaternary structures, a single functional unit composed of more than one amino acid chain. For example, hemoglobin functions as a tetramer, composed of two alpha and two beta subunits.   Even larger structures can be built when a globular protein associates with one or more additional proteins. For example, an actin filament is formed when many globular actin monomers join together to create long helical protein strands.  Unlike compact globular proteins, fibrous proteins are often located in the extracellular matrix, provide structure, and form extended shapes. Fibrous proteins are usually composed of either alpha-helices or beta-sheets, but rarely a mix of both. They often have hydrophobic amino acids on their outer surfaces that interact with other monomers to form larger structures. For example, collagen is a fibrous protein composed of an extended alpha helix.  Three helices wind around each other to make a structure called a coiled-coil. Collagen fibrils provide structure and flexibility in connective tissues. The protein fibroin is an example of a fibrous protein composed of beta-sheets and is the protein in silk which allows the silk strands to be both flexible and strong. 

3.5:

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes – globular or fibrous. These two types differ in their shapes and solubilities.

Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be soluble in the aqueous cellular environment. They are also sensitive to changes in their environment, such as pH and temperature.  Hemoglobin, immunoglobulin, and protein kinase A are examples of globular proteins.

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures.  They are may contain repetitive units and usually consist either of alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural.  Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are not typically soluble in water; however, they may be soluble in strong acids or bases.  Collagen, keratin, elastin, silk, and fibrin are examples of fibrous proteins. 

Suggested Reading

  1. 1PDB ID: 1GZX
    Paoli, M., Liddington, R., Tame, J., Wilkinson, A., Dodson, G. (1996)  Crystal Structure of T State Haemoglobin with Oxygen Bound at All Four Haems. J Mol Biol 256: 775
  2. 2PDB ID: 3UA0
    He, Y.X., Zhang, N.N., Li, W.F., Jia, N., Chen, B.Y., Zhou, K., Zhang, J., Chen, Y., Zhou, C.Z.
  3. (2012) N-Terminal Domain of Bombyx mori Fibroin Mediates the Assembly of Silk in Response to pH Decrease. J Mol Biol 418: 197-207
  4. H.M. Berman, J. Westbrook, Z. Feng, G. Gilliland, T.N. Bhat, H. Weissig, I.N. Shindyalov, P.E. Bourne. (2000) The Protein Data Bank Nucleic Acids Research, 28: 235-242.
  5. D. Sehnal, A.S. Rose, J. Kovca, S.K. Burley, S. Velankar (2018) Mol*: Towards a common library and tools for web molecular graphics MolVA/EuroVis Proceedings. doi:10.2312/molva.20181103