Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Paweł Dąbrowski-Tumański"'
Publikováno v:
Molecules, Vol 28, Iss 22, p 7462 (2023)
AlphaFold is a groundbreaking deep learning tool for protein structure prediction. It achieved remarkable accuracy in modeling many 3D structures while taking as the user input only the known amino acid sequence of proteins in question. Intriguingly
Externí odkaz:
https://doaj.org/article/696e35bbf1f54cb3b27c506a443ea47c
Publikováno v:
Polymers, Vol 13, Iss 22, p 3988 (2021)
Complex lasso proteins are a recently identified class of biological compounds that are present in considerable fraction of proteins with disulfide bridges. In this work, we look at complex lasso proteins as a generalization of well-known cysteine kn
Externí odkaz:
https://doaj.org/article/467f55480cd4499fad788c704f888529
Autor:
Agnese Barbensi, Naya Yerolemou, Oliver Vipond, Barbara I. Mahler, Pawel Dabrowski-Tumanski, Dimos Goundaroulis
Publikováno v:
Symmetry, Vol 13, Iss 9, p 1670 (2021)
Understanding how knotted proteins fold is a challenging problem in biology. Researchers have proposed several models for their folding pathways, based on theory, simulations and experiments. The geometry of proteins with the same knot type can vary
Externí odkaz:
https://doaj.org/article/9e3dd10b91bf423ea7e59de60c4d9f06
Publikováno v:
PLoS Computational Biology, Vol 14, Iss 3, p e1005970 (2018)
The folding of proteins with a complex knot is still an unresolved question. Based on representative members of Ubiquitin C-terminal Hydrolases (UCHs) that contain the 52 knot in the native state, we explain how UCHs are able to unfold and refold in
Externí odkaz:
https://doaj.org/article/4ec51659141f42f0ade890c2cfb4b0c2
Publikováno v:
Polymers, Vol 11, Iss 4, p 707 (2019)
The shape and properties of closed loops depend on various topological factors. One of them is loop-threading, which is present in complex lasso proteins. In this work, we analyze the probability of loop-threading by the tail and its influence on the
Externí odkaz:
https://doaj.org/article/86146487050643d0b9ab6d2f3039435f
Publikováno v:
TASK Quarterly, Vol 20, Iss 4 (2016)
The folding of knotted proteins remains a mystery both for theoreticians and experimentalists. Despite the development of new models, the driving force for self-tying remains elusive and the principle of minimal frustration cannot be reproduced in si
Externí odkaz:
https://doaj.org/article/7b8713cf29124981ab4cfa91170a896b
Publikováno v:
PLoS ONE, Vol 11, Iss 11, p e0165986 (2016)
We analysed the structure of deeply knotted proteins representing three unrelated families of knotted proteins. We looked at the correlation between positions of knotted cores in these proteins and such local structural characteristics as the number
Externí odkaz:
https://doaj.org/article/32aead7c514c42668cb2df4b78e202b7
Publikováno v:
Polymers, Vol 9, Iss 9, p 454 (2017)
In this review, we provide an overview of entangled proteins. Around 6% of protein structures deposited in the PBD are entangled, forming knots, slipknots, lassos and links. We present theoretical methods and tools that enabled discovering and classi
Externí odkaz:
https://doaj.org/article/434dc344c33143e299b0fb1514029f85
Publikováno v:
TASK Quarterly, Vol 18, Iss 3 (2014)
Proteins with a non-trivial topological structure are currently well recognized, while a knotted protein chain represents a new motif in protein three dimensional folds. Recent comprehensive analysis of the Protein Data Base shows that knotted protei
Externí odkaz:
https://doaj.org/article/7b7d7f4c50224cb4a4e70a71788d31f6
Autor:
Paweł Włodarczyk-Pruszyński, Piotr Byrski, Paweł Dąbrowski-Tumański, Mikołaj Sacha, Mikolaj Chrominski, Mikołaj Błaż, Stanisław Jastrzębski, Rafał Loska
The central challenge in automated synthesis planning is to be able to generate and predict outcomes of a diverse set of chemical reactions. In particular, in many cases, the most likely synthesis pathway cannot be applied due to additional constrain
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c644c2b10b1cdbbb788cfc2753c53c9c
http://arxiv.org/abs/2006.15426
http://arxiv.org/abs/2006.15426
