Domains, Motifs, and Folds in Protein Structure
Protein are frequently described as consisting from several structural units.
- A structural domain is an element of the protein's overall structure that is self-stabilizing and often folds independently of the rest of the protein chain. Many domains are not unique to the protein products of one gene or one gene family but instead appear in a variety of proteins. Domains often are named and singled out because they figure prominently in the biological function of the protein they belong to; for example, the "calcium-binding domain of calmodulin". Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeras.
- The structural and sequence motifs refer to short segments of protein three-dimensional structure or amino acid sequence that were found in a large number of different proteins.
- The supersecondary structure refers to a specific combination of secondary structure elements, such as beta-alpha-beta units or helix-turn-helix motif. Some of them may be also referred to as structural motifs.
- Protein fold refers to the general protein architecture, like helix bundle, beta-barrel, Rossman fold or different "folds" provided in the Structural Classification of Proteins database.
Despite the fact that there are about 100,000 different proteins expressed in eukaryotic systems, there are many fewer different domains, structural motifs and folds.
Read more about this topic: Protein Structure
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