Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Gabriele Pozzati"'
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
The accuracy of AlphaFold decreases with the number of protein chains and the available GPU memory limits the size of protein complexes that can be predicted. Here, the authors show that complexes with 10–30 chains can be assembled from predicted s
Externí odkaz:
https://doaj.org/article/ba16c3928c6b4e7b987cfb650ae54d3b
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
Predicting the structure of protein complexes is extremely difficult. Here, authors apply AlphaFold2 with optimized multiple sequence alignments to model complexes of interacting proteins, enabling prediction of both if and how proteins interact with
Externí odkaz:
https://doaj.org/article/8aa778e1b2c04520946147bebf4857a3
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-1 (2022)
Externí odkaz:
https://doaj.org/article/9ac0d39b75974ff0bf919ea203949ef0
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 90:1493-1505
Scoring docking solutions is a difficult task, and many methods have been developed for this purpose. In docking, only a handful of the hundreds of thousands of models generated by docking algorithms are acceptable, causing difficulties when developi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5ebce5bab00e865c7550ec24ec5513bf
https://doi.org/10.1002/prot.26330
https://doi.org/10.1002/prot.26330
Publikováno v:
Bioinformatics
Motivation In the last decade, de novo protein structure prediction accuracy for individual proteins has improved significantly by utilising deep learning (DL) methods for harvesting the co-evolution information from large multiple sequence alignment
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::88c6252c474933932e8e4080f8df675b
https://doi.org/10.1093/bioinformatics/btab760
https://doi.org/10.1093/bioinformatics/btab760
Publikováno v:
Nature Communications. 13
AlphaFold can predict the structure of single- and multiple-chain proteins with very high accuracy. However, the accuracy decreases with the number of chains, and the available GPU memory limits the size of protein complexes which can be predicted. H
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::303706d7a4f9d4da7b03397e6d3eb722
https://doi.org/10.1038/s41467-022-33729-4
https://doi.org/10.1038/s41467-022-33729-4
Autor:
Richard A. Scheltema, Danish Memon, Pedro Beltrao, Alistair Dunham, David F. Burke, Zhu W, Abigail Keller, Inigo Barrio-Hernandez, Petras J. Kundrotas, James E. Bruce, Gabriele Pozzati, Albanese P, Shenoy A, Arne Elofsson, Patrick Bryant, Alexander Leitner
All cellular functions are governed by complex molecular machines that assemble through protein-protein interactions. Their atomic details are critical to the study of their molecular mechanisms but fewer than 5% of hundreds of thousands of human int
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e4ba4768703354be860646795f38831
https://doi.org/10.1101/2021.11.08.467664
https://doi.org/10.1101/2021.11.08.467664
Predicting the structure of interacting protein chains is fundamental for understanding the function of proteins. Here, we examine the use of AlphaFold2 (AF2) for predicting the structure of heterodimeric protein complexes. We find that using the def
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::609b2829f3c8a9450020813eb85db99f
https://doi.org/10.21203/rs.3.rs-951605/v1
https://doi.org/10.21203/rs.3.rs-951605/v1
Publikováno v:
Nature communications. 13(1)
Predicting the structure of interacting protein chains is a fundamental step towards understanding protein function. Unfortunately, no computational method can produce accurate structures of protein complexes. AlphaFold2, has shown unprecedented leve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6584c25cd01d01514d5b2c8241da4d45
https://pubmed.ncbi.nlm.nih.gov/35332153
https://pubmed.ncbi.nlm.nih.gov/35332153
Scoring docking solutions is a difficult task, and many methods have been developed for this purpose. In docking, only a handful of the hundreds of thousands of models generated by docking algorithms are acceptable, causing difficulties when developi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a16be64640a948cff880b7e935a53d03
https://doi.org/10.22541/au.163254390.01798129/v1
https://doi.org/10.22541/au.163254390.01798129/v1