AlphaFold

Zecheng Zhang1, Weitong Ren2, Liangxu Xie3

  • 1Hong Kong Baptist University, Department of Physics, 224 Waterloo Road, Kowloon Tong, Hong Kong SAR, China.

PubMed
概括

蛋白质折叠拓影响了蛋白质的动态. 人工智能模型显示,折叠速度较慢的蛋白质也具有有限的灵活性,这表明跨物种蛋白质结构中的普遍物理原理.

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Protein Folding01:25

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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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