WikiJournal of Science/The TIM barrel fold/XML

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    <full_title>WikiJournal of Science/The TIM barrel fold</full_title>
    <issn media_type='electronic'>2002-4436 / 2470-6345 / 2639-5347</issn>
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     <title>The TIM barrel fold</title>
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    <publication_date media_type='online'>     
     <resource> of Science/The TIM barrel fold</resource>
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This is an open access article distributed under the&nbsp;[ Creative Commons Attribution License], which permits unrestricted use, distribution, and reproduction, provided the original author and source are credited.</license-p>
Proteins are biological polymers composed of linear chains of 20 different amino acids. The sequence of amino acids for every protein is unique, and guides its folding into intricate 3-dimensional shapes, known as protein folds. The TIM barrel is one such fold, and is characterized by an interior 8-stranded β-barrel, surrounded and enclosed by 8 α-helices. TIM barrels are named after triose phosphate isomerase (TIM), an enzyme first structurally characterized in 1975, which lends its name to the fold. TIM barrels are prevalent in all forms of life, and across diverse metabolic pathways, with over 10% of all enzymes adopting this fold. The majority of TIM barrels are thought to have evolved from a common ancestor through gene duplication and domain fusion processes. TIM barrels have been created by protein engineers using preexisting half-barrel templates and ''de novo'', without an existing template. This review will discuss the topological, structural, evolutionary, and design characteristics of TIM barrels in detail.