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ColabFold: making protein folding accessible to all

ColabFold offers accelerated prediction of protein structures and complexes by combining the fast homology search of MMseqs2 with AlphaFold2 or RoseTTAFold. ColabFold’s 40−60-fold faster search and optimized model utilization enables prediction of close to 1,000 structures per day on a server with o...

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Autores principales: Mirdita, Milot, Schütze, Konstantin, Moriwaki, Yoshitaka, Heo, Lim, Ovchinnikov, Sergey, Steinegger, Martin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group US 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9184281/
https://www.ncbi.nlm.nih.gov/pubmed/35637307
http://dx.doi.org/10.1038/s41592-022-01488-1
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author Mirdita, Milot
Schütze, Konstantin
Moriwaki, Yoshitaka
Heo, Lim
Ovchinnikov, Sergey
Steinegger, Martin
author_facet Mirdita, Milot
Schütze, Konstantin
Moriwaki, Yoshitaka
Heo, Lim
Ovchinnikov, Sergey
Steinegger, Martin
author_sort Mirdita, Milot
collection PubMed
description ColabFold offers accelerated prediction of protein structures and complexes by combining the fast homology search of MMseqs2 with AlphaFold2 or RoseTTAFold. ColabFold’s 40−60-fold faster search and optimized model utilization enables prediction of close to 1,000 structures per day on a server with one graphics processing unit. Coupled with Google Colaboratory, ColabFold becomes a free and accessible platform for protein folding. ColabFold is open-source software available at https://github.com/sokrypton/ColabFold and its novel environmental databases are available at https://colabfold.mmseqs.com.
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spelling pubmed-91842812022-06-11 ColabFold: making protein folding accessible to all Mirdita, Milot Schütze, Konstantin Moriwaki, Yoshitaka Heo, Lim Ovchinnikov, Sergey Steinegger, Martin Nat Methods Brief Communication ColabFold offers accelerated prediction of protein structures and complexes by combining the fast homology search of MMseqs2 with AlphaFold2 or RoseTTAFold. ColabFold’s 40−60-fold faster search and optimized model utilization enables prediction of close to 1,000 structures per day on a server with one graphics processing unit. Coupled with Google Colaboratory, ColabFold becomes a free and accessible platform for protein folding. ColabFold is open-source software available at https://github.com/sokrypton/ColabFold and its novel environmental databases are available at https://colabfold.mmseqs.com. Nature Publishing Group US 2022-05-30 2022 /pmc/articles/PMC9184281/ /pubmed/35637307 http://dx.doi.org/10.1038/s41592-022-01488-1 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Brief Communication
Mirdita, Milot
Schütze, Konstantin
Moriwaki, Yoshitaka
Heo, Lim
Ovchinnikov, Sergey
Steinegger, Martin
ColabFold: making protein folding accessible to all
title ColabFold: making protein folding accessible to all
title_full ColabFold: making protein folding accessible to all
title_fullStr ColabFold: making protein folding accessible to all
title_full_unstemmed ColabFold: making protein folding accessible to all
title_short ColabFold: making protein folding accessible to all
title_sort colabfold: making protein folding accessible to all
topic Brief Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9184281/
https://www.ncbi.nlm.nih.gov/pubmed/35637307
http://dx.doi.org/10.1038/s41592-022-01488-1
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