期刊
JOURNAL OF CHEMICAL INFORMATION AND MODELING
卷 61, 期 10, 页码 4827-4831出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jcim.1c01114
关键词
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AlphaFold 2 (AF2) successfully predicted the structures of many challenging protein targets using novel deep learning and a sophisticated fold recognition algorithm. It leverages the completeness of the library of single domain PDB structures, learned local side chain packing rearrangements, and can refine proteins to high resolution. The benefits and limitations of its ability to predict the structures of many more proteins at or close to atomic detail are discussed.
AlphaFold 2 (AF2) was the star of CASP14, the last biannual structure prediction experiment. Using novel deep learning, AF2 predicted the structures of many difficult protein targets at or near experimental resolution. Here, we present our perspective of why AF2 works and show that it is a very sophisticated fold recognition algorithm that exploits the completeness of the library of single domain PDB structures. It has also learned local side chain packing rearrangements that enable it to refine proteins to high resolution. The benefits and limitations of its ability to predict the structures of many more proteins at or close to atomic detail are discussed.
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