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DeepMind is known to have trained the program on over 170,000 proteins from the Protein Data Bank, a public repository of protein sequences and structures.The program uses a form of attention network, a deep learning technique that focuses on having the AI identify parts of a larger problem, then piece it together to obtain the overall solution. [2]
Constituent amino-acids can be analyzed to predict secondary, tertiary and quaternary protein structure. This list of protein structure prediction software summarizes notable used software tools in protein structure prediction, including homology modeling, protein threading, ab initio methods, secondary structure prediction, and transmembrane helix and signal peptide prediction.
Dr Andriy Kryshtafovych, one of the panel of scientific adjudicators, described the achievement as "truly remarkable", and said the problem of predicting how proteins fold had been "largely solved". [76] [77] [78] In July 2021, the open-source RoseTTAFold and AlphaFold2 were released to allow scientists to run their own versions of the tools.
John Michael Jumper (born 1985) [1] is an American chemist and computer scientist. He currently serves as director at Google DeepMind. [2] [3] [4] Jumper and his colleagues created AlphaFold, [5] an artificial intelligence (AI) model to predict protein structures from their amino acid sequence with high accuracy. [6]
This page was last edited on 26 November 2021, at 16:57 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply.
Name Underlying data model Full and Latest SysML support Full and Latest UML support XMI Automated document generation OSLC support Can be integrated with Astah: Yes Partial ...
TensorFlow is an open source software library powered by Google Brain that allows anyone to utilize machine learning by providing the tools to train one's own neural network. [2] The tool has been used to develop software using deep learning models that farmers use to reduce the amount of manual labor required to sort their yield, by training ...
An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).